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Amanda's MCAT Flashcards > BioChem > Flashcards

BioChem Flashcards

1
Q

What is the sterochemistry of all chiral carbons in Eukaryotes?

A

L-amino acid (S configuration)

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2
Q

What is the isoelectric point?

A

The pH when the molecule is electrically neurtral

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3
Q

How does proline behave in secondary structres?

A

It si rigid so it introduced kinks into the alpha-helices or creates turns in the Beta-pleated sheets

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4
Q

What is the difference between heat and solutes denaturing proteins?

A

heat: disrupts hydrophobic bonds
solutes: disrupt secondary, tertiary, and quaternary structures

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5
Q

Is polypeptide formation a condensation or hydration rxn?

A

condensation

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6
Q

What is a tightly bound cofactor or coenzyme that is necessary for enzyme function called?

A

prosthetic groups

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7
Q

What are the two differences between the Michaelis-Menten plot and the Lineweaver-Burk plot?

A
  1. Michaelis-Menten plot is v vs. [S] and has a hyperbolic shaped curve
  2. Lineweaver-Burk plot is (1/v) vs. (1/[S]), which is a straight line
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8
Q

What does a high kcat and a small Km mean?

A

high catalytic efficiency

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9
Q

What is the ideal temp for most enzymes in the body?

A

37 degrees celcius=98.6 degrees F” 310 K

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10
Q

What is the ideal pH for…

  1. Most enzymes
  2. Gastric enzymes
  3. Pancreatic enzymes
A
  1. 7.4
  2. 2
  3. 8.5
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11
Q

Where can mixed inhibitors bind and how does the difference in binding change the Km of enzyme? How does Vmax change?

A

Binds to allosteric site

  1. Bind to enzyme–> increase Km value
  2. Bind to enzyme-substrate complex –> lower Km

Vmax for both decreases

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12
Q

Where do uncompetitive inhibitors bind and how do they influence Km and Vmax?

A

They bind to an allosteric site. Bind to enzyme-substrate complex and lock the substrate in enzyme.

Km and Vmax both decrease

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13
Q

What are two possible methods for irreversible inhibition?

A
  1. active site is made unavailable
  2. enzyme is permanently altered
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14
Q

What are the two domains of zymogens and why do they have these domains?

A

They have a catalytic (active) and a regulatory domain

Zymogens are secreted in inactive form because dangerous and regulatory domain can be removed or alterd to expose active site

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15
Q

What are the 5 structural proteins?

A
  1. Collagen: provide strength/flexibility, makes up extracellar matrix of connective tissue
  2. Elastin: stretch and recoil, component of extracelluar matrix of connective tissue
  3. Keratin: intermediate filament proteins in epithelial cells/mechanical integrity of cell/regulatory proteins
  4. Actin: microfilaments and thin filaments in myofibrils. Is polar to allow motor proteins to travel undirectionally/most abundant protein in eukaryotes
  5. Tubulin: makes up microtubules, have polarity (negative end is near nucleus and positive end is in the periphery of cell)
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16
Q

What are three motor protons and their primary functions?

A
  1. Myosin: interact with actin/cellular transport/involved in thick filaments in myofibril

2/3. Kinesins and dyneins: vesicle transport

  • Kinesin: align chromosoms during metaphase
  • Dyneins: involved in sliding movement of cilia and flagella

-

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17
Q

What are two difference between cytoskeletal and motor proteins?

A
  1. Cytoskeletal tend to be fibrous with repeating domains (motifs)
  2. Motor proteins have ATPase activity and binding heads
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18
Q

What are the three major families of cell adhesion molecules?

A
  1. Cadherins: glycoproteins that mediate Ca-dependent cell adhesion
  2. Integrins: two membrane spanning proteins\play role in cell signaling (cell-cell adhesion)
  3. Selectins: bind to carbohydrates that project from cell surfaces/ play role in host defense
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19
Q

Define opsonization?

A

antibody marks pathogen for destruction

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20
Q

Define agglutinating?

A

clumbing together the antigen and antibody into a large insoluble protein complex that can be phagocytized

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21
Q

What two types of bonds hold the heavy and light chains of antibodies together?

A

disulfide bonds and noncovalent bonds

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22
Q

What are the two domains of an antibody? Function for each?

A

V-domain: bind to antigen

C-domain: activate complememt/phagocytosis

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23
Q

What are four steps in GPCR pathway?

A
  1. Ligand binding enages the G protein
  2. GDP–> GTP, alpha unit dissociates from beta and gamma
  3. activated alpha subunit alters the activity of adenylate cyclase or phospholipase C
  4. GTP is dephosphorylated to GDP, alpha subunit rebinds to gamma and beta
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24
Q

What are the three main types of G proteins?

A
  1. Gs=stimulates adenylate cyclase, increases cAMP in cell
  2. Gi=inhibits adenylate cyclase, decreases cAMP in cell
  3. Gq=activates phospholipase C, which cleaves a phospholipid from the membrane to form PIP2 –> cleaved inton DAG and IP3
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25
Q

What are two difference between a Native PAGE and SDS-PAGE?

A
  1. Native maintains shape of protein so complete protein can be recoved after analysis and more accurately determines globular size of protein
  2. SDS- denatures protein and masks charge to can compare size of protein
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26
Q

What is one important concept for Size exclusion chromatography?

A

larger molecules elute first bc small molecules are trapped in small pores of beads

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27
Q

What are two drawbacks to affinity chromatography?

A
  1. protein of interest may not elute because affinity is too high
  2. protein may be permanently bound to the free receptor in the elutent
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28
Q

What is the primary method of determining protein structure?

A

X-ray crystallography but NMR can be used as well

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29
Q

What are two ways amino acids that compose a protein can be determined?

A
  1. amino acids that compose a protein can be determined by protein hydrolyisis and then chromatographic analysis
  2. Use edman degradation: selectively and sequentially removes the N-terminal amino acids and then anaylze via mass spectroscopy
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30
Q

What are four ways protein concentration can be detemrined? Which one is most common?

A
  1. UV spectroscopy: bc proteins can have aromatic side chains so do not need any treatment, but sensitive to contaminants
  2. Colorimetric changes –> BCA assay, Lowry reagent assay, Bradford assay
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31
Q

What die does Bradford Assay use and how does it work?

A
  1. Coomassie Brilliant Blue dye (green-brown)
  2. Gives up protons when bind to amino acids and will turn blue
  3. more protein, stronger blue color
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32
Q

Equation for vmax?

A

vmax=[E]xkcat

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33
Q

What might be two plausible explainations if you detect a low activity with a high concentration of protein when using affinityn chromatography?

A
  1. protein is inactive
  2. Protein elutes off of an affinity collumn by binding free ligand. The binding might not have be reversed for the active site to be occupied for the free ligand so stayed on column
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34
Q

Name?

A

D-fructose

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35
Q

How do you find the number of steroisomers?

A

2^n

n=the number of chiral carbons

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36
Q

What is the difference between a diastereomers and epimers?

A

Epimers are diastereomers but epimers differ in configuration at exactly one chiral center

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37
Q

How can monosaccharides for cyclic hemiacetals or hemiketals?

A

the hydroxyl serves as a nucleophile and the carbonly group is the electrophile

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38
Q

What is the difference between and alpha-anomer and a beta-anomer?

A

Alpha: has the -OH of the C-1 trans to the CH2OH (axial)

Beta: has the -OH group of the C-1 cis to the -CH2OH (equitorial)

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39
Q

What is Mutarotation?

A

Hemiacetal rings ossilate btw either alpha or beta anomer

the alpha-anomer is less favored bc the hydroxyl of anomeric carbon is axial

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40
Q

What are oxidized aldehydes called? Are they strong reducing or oxidizing agents?

A

Aldonic acids –> strong reducing agents

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41
Q

What two reagents are used to detect reducing sugars?

A
  1. Tollens’ reagent: Tollen’s reagent is reduced to produce a silver mirror in the presence of aldehydes
  2. Benedict’s reagent: form a red ppt. This test is specific for glucose
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42
Q

Which one of the three most important disaccharides is this?

A

Sucrose (glucose alpha 1, 2 fructose)

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43
Q

Which one of the three most important disaccharides is this?

A

Lactose (galactose Beta 1,4 glucose)

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44
Q

Which one of the three most important disaccharides is this?

A

Maltose (glucose alpha 1,4 glucose)

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45
Q

What are three characteristics of cellulose?

A
  1. Beta D glucose linked by B 1,4 glycosidic bonds
  2. H-bonds holding polymer chains together for support–> very strong
  3. humans do not have cellulase
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46
Q

What are four characteristics of starch?

A
  1. alpha D glucose linked by alpha 1,4 glycosidic bonds
  2. plants store starch as amylose
  3. amylopectin is a starch but has branches bia alpha 1,6 glycosidic bonds
  4. Broken down by alpha and beta amylase
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47
Q

What are three characteristics of glycogen?

A
  1. Similar to starch but with more alpha 1,6 glycosidic bonds
  2. more branching –> decrease intermolecular bonding –> more soluble in water so more glucose to be stored in body
  3. Branching allows gylcogen phosphorylase to cleave at mutliple nonreducing ends and phosyphorylate them
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48
Q

What are three types of structural lipids?

A
  1. Phospholipids
  2. Glycerophospholipids
  3. Spingolipids
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49
Q

What are three components of Phospholipids?

A
  1. a phosphate
  2. alcohol which is joined to a 3)hydrophobic fatty acid by a phophodiester linkage
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50
Q

What are three components of Glycerophospholipids? How are they bonded together?

A
  1. phospholipid that contains a glycerol back bone bonded by ester linages to two fatty acids and by a phosphodiester bond to a polar head group
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51
Q

What are the three components of sphingolipids?

A
  1. sphingosine or sphingoid backbone instead of a glycerol one
  2. long chain, non-polar fatty acid tails
  3. polar head group
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52
Q

What are two traits of waxes?

A
  1. esters of long chain fatty acids with long chain alcohols
  2. help animals and plants prevent dehydration
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53
Q

What are four signaling lipids?

A
  1. Terpenes/Terpenoids
  2. Steroids
  3. Prostaglandins
  4. Fat-soluble vitamins
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54
Q

What are two traits of cholesterol?

A
  1. amphipathic
  2. a low temps keeps membrane from freezing and at high temps keeps memebrane intact
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55
Q

What is the defining structure of steroids?

A

three cyclohexane rings and one cyclopentane ring

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56
Q

What are 3 traits of prostaglandins?

A
  1. paracrine and autocrine signaling molecules (not endocrine)–> they affect regions close to where they are produced rather than affecting entire body
  2. regulate synthesis of cAMP
  3. affect smooth muscle contraction, body temp, fever, pain, sleepwake cycle
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57
Q

What are three main traits of vitamin A?

A
  1. important for vision, growth, immune function
  2. Vit A/carotene is metabolized to retinal
  3. Retinol is the storage form of vit A and is oxidized to retinoic acid which regulate gene expression in epithelial development
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58
Q

What are three main traits of vitamin D?

A
  1. can be consumed or formed in UV light driven rxn in skin
  2. Vit D/cholecalciferol: in liver and kidney is converted into calcitriol which increases Ca and phosphate uptake in intestines to promote bone production
  3. lack of vit D can result in rickets, which is curved long bones and impeded growth in children
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59
Q

What are three traits of vitamin E?

A
  1. also known as tocopherols
  2. act has biological antioxidants
  3. aromatic rings destroy free radicles, preventing oxidative damage (ex:cancer)
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60
Q

What are three traits of vitamin K?

A
  1. called phylloquinone and menaquinones
  2. allows for postranslational modification of prothrombin (clotting factor in blood)
  3. required to introduce Ca-binding sites on calcium dependent proteins
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61
Q

What are two lipids involved in energy storage?

A
  1. Triacylglycerols
  2. Free Fatty Acids
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62
Q

What are three traits of triacyglycerols?

A
  1. three fatty acids bonded by ester linkages to glycerol
  2. adipocytes store triaglycerides
  3. the carbon atoms in lipids are more reduced than carbohydrates so they release 2x as much energy
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63
Q

What are two traits of free fatty acids?

A

1) esterfied fatty acids with a free carboxylate group
2) circulate in the blood by noncovalently bonding to albumin

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64
Q

What is saponification?

A

ester hydrolysis of trycylglycerols using a strong base (lye–> NaOH/KOH)–> leaving glycerol and fatty acid salt (soap)

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65
Q

What is the function of soap and how does it work?

A

It is a surfactant and lowers the surface tension of the liquid surface (detergent and emulsiferi)

aggregates of soap with hydrophobic tails turn inward with hydrophilic tails outward (micelles) to dissolve lipid-soluble molecules, watch away water and the formation of a colloid, combo of two phases

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66
Q

What two susbtances in body allow the formation of micelees?

A

fatty acids and bile salts secreted from gallbladder

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67
Q

What are topoismerases? What is one example?

A

They are involved in DNA replication and mRNA synthesis

ex: negative supercoils into the DNA molecules. facilitate DNA replication by keeping the strands separated and untangled

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68
Q

What is the main function of flippases?

A

Responsible for the movement of phospholipids between the layers of the plasma membrane because it is otherwise energetically unfavorable

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69
Q

What are the two structures phospholipids spontaneously form into?

A

micelles (monolayer vessicles) and liposomes (bilayer vessicles)

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70
Q

What are desmosomes and Hemidesmosomes?

A
  1. Desmosomes: bind adjacent cells by anchoring to the cytoskeleton and are formed by interactions btw transmembrane proteins associated with intermediate filaments inside adjacent cells
  2. Hemisomes: main function is to attach epithelial cells to underlying structures
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71
Q

What is osmotic pressure? How does it relate to the direction of water flow?

A
  1. pressure applied to a pure solvent to prevent osmosis
  2. water will move towards area with highest osmotic pressure
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72
Q

What is pinocytosis?

A

endocytosis of fluid and disolved substances

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73
Q

What 4 lipids make up the plasma membrane?

A
  1. Triagylcerides and fatty acids–> precursor for phospholipids
  2. Glycerophospholipids: replace one fatty acid with phosphate group
  3. cholesterol
  4. wax
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74
Q

What is the difference between the inner mitochondrial membrane and other biological membranes? What is the pH gradient btw cytoplasm and intermembrane space?

A
  1. Innermembrane space lacks cholesterol
  2. no pH gradient bc the outer mitochondrial membrane has a high permeability for molecules
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75
Q

What is the Nernst Equation?

A

E=(61.5/z)log ([ion]out/[ion]in)

z=charge of ion

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76
Q

What are 4 difference/similarities between GLUT 2 and 4?

A
  1. GLUT 2 is in hepatocytes and pancreatic cells and GLUT4 is in adipose and muscle cells
  2. The Km for GLUT2 is higher (has first order kinetics) than for GLUT4 (zero order kinetics)
  3. GLUT4 is responsive to insulin bit GLUT2 is not (but it serves as a glucose sensor to cause release of insulin in pacreatic B-cells)
  4. GLUT4 is saturated when blood glucose levels are just a bit higher than normal (still only permit a constant flow of glucose so increase transport but increase number of transporters). GLUT2 cannot be saturated under normal conditions
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77
Q

What are the 2 difference between Hexokinase and Glucokinases?

A
  1. Hexokinase found in most tissue and glucokinases present in hepacytes and pacreatic B-iselt cells
  2. Hexokinase has low Km, glucokinase has high Km
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78
Q

What is the main function of lactate dehydrogenase?

A
  1. reduce pyruvate to lactate and make more NAD+, which replenishes the oxidized coenzyme for glyceraldehyde 3 phosphate
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79
Q

What are the three steps for fructose metabolism?

A
  1. liver phosphorylates fructose using furctokinase to trap inside cells.
  2. Fructose 1-phosphate is cleaved into glyceraldehyde(can be phosphorylated into G3P and DHAP by aldolase
  3. go to glycolysis, glycogenesis, glucoeogenesis
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80
Q

What are these called?

  1. thiamine
  2. pyrophosphate
  3. lipoic acid
  4. CoA
  5. FAD
  6. NAD+
A

cofactors

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81
Q

What are 4 traits of the Pyruvate dehydrogenase reaction?

A
  1. Pyruvate enter mitochondira and converted to acetyl-CoA for entry into the citric acid cycle
  2. pyruvate hydrolysis is inhibited by acetly-CoA and pyruvate is converted into oxaloacetate by pyruvate carboylase to enter gluconeogensis
  3. pyruvate dehydrogenase in liver is activated by insulin
  4. reactants are pyruvate, NAD+, CoA and products are NADH, CO2, and acetyl CoA
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82
Q

What is glycogenesis?

A

forming glycogen

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83
Q

What are 3 facts about glycogen synthase?

A
  1. rate-limiting enzyme of glycogen synthesis and forms the alpha-1,4 glycosidic bond found in linear glucose
  2. stimulated by G6P and insulin
  3. inhibited by epinephrine and glucagon
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84
Q

What are 2 facts about branching enzyme?

A
  1. introduces alpha 1-6 linked branches into the granile as it grows
  2. role in glycogensis
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85
Q

What are 3 facts about glycogenolysis?

A
  1. process of breaking down glycogen using glycogen phosphorylase
  2. glycogen phosphorylase is activated by glucagon in the liver and by AMP/Epinephrin in the skeletal muscles
  3. cannot break down alpha 1-6 bond so stops near the outmost branch points
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86
Q

What are 3 facts about debranching enzymes?

A
  1. two enzyme complex that deconstructs the branches in glycogen that have been exposed to glycogen phosphorylase
  2. breaks alpha 1,4 bonds adjacent to the branch points and moves the small oligo-glucose chains that is releases to exposed end of other chain, form new alpha 1,4 bond to a longer link.
  3. role in glycogenolysis
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87
Q

What is the difference btw glucogenic and ketogenic amino acids?

A

Glucogenic aa (all except leucine and lysine) can be converted into intermediates and feed into gluconeogenesis

ketogenic aa can be converted into ketone bodies which can be used as alternative fuel

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88
Q

Under what two conditions should the body carry out gluconeogensis?

A
  1. when a person is fasting for more than 12 hours
  2. hepatic and renal cells must have enough energy to drive the process of glucose creation, which require succificent fat stores and B oxidation

mostly in the liver

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89
Q

How does acetyl-CoA shift the metabolism of pyruvate?

A
  1. Acetly-CoA inhibits pyruvate dehyrogenase complex while activating pyruvate carboxylase. Shift from burning pyruvate in the citric acids cycle to creating new glucose molecules for the rest of the body. The acetle CoA from this regulations comes from B-oxidation (fatty acid oxidation)and not glycolysis (bc would just burn the glucose that is being generated)
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90
Q

What are the two main functions of the pentose phosphate pathway?

A
  1. producetion of NADPH
  2. source ofr ribose-5-phosphate for nucleotide synthesis
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91
Q

What is glutathione?

A

reducing agent that can help reverse radical formation before damage is done

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92
Q

What is the overall reaction of the pyruvate dehydrogenase complex?

A

Pyruvate +CoA-SH +NAD+–> Acetyl-CoA +CO2+NADH+H+

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93
Q

What is the main purpose of the citric acid cycle?

A

complete oxidation of carbons in intermediates to CO2 so can have reductions coupled with CO2 formation to form NADH and FADH2 for ETC

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94
Q

What are the three main sites of regulation for citric acid cycle? Which one is the rate limiting enzyme?

A
  1. Citrate synthase: Inhibitors are ATP, NADH, succinyl-CoA and citrate/ no activators
  2. Isocitrate dehydrogenase (rate limiting enzyme): Inhibitors are ATP and NADH, activators are ADP and NAD+
  3. Alpha-ketoglutarase complex: Inhibitors are ATP, NADH, succinyl-CoA/ activiators are ADP, Ca2+
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95
Q

What are the the 3 products yeilds from citric acid cycle? How many ATPs do they produce?

A
  1. 3 NADH–> 10 ATP
  2. 1FADH2–> 1.5 ATP
  3. 1 GTP–> 1ATP

(mutliple by two for one glucose molecule)

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96
Q

What are the 4 different complexes in the ETC?

A
  1. Complex I: transfer of electrons from NADH to CoQ. First site of proton pump (4 protons)
  2. Complex II: FADH2 reduced by iron-sulfate protein in CoQ. No hydrogen pumping here
  3. Complex III: transfers of electrons from CoQ to cytochrome c. proton pump here (4 protons)
  4. Complex IV: transfer of electron from cytochrome c to oxygen. proton pump here (two protons)
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97
Q

What are the two important subunits of CoQ out of the 20 subunits?

A
  1. proteins that has a iron-sulfer cluster
  2. Flavoprotein that oxidizes NADH. Flavoprotein has a coenzyme called FMN.
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98
Q

What are the 2 shuttle mechanisms that cause a range of 30-32 ATPs to be produced?

A

Shuttle mechanism: transfers high energy electrons of NADH to a carrier than can cross the inner mitochondrial membrane because NADH cannot cross inner mitchondrial membrane

Gylcerol 3-phosphate Shuttle: allow NADH produces in cytosol to be used in ETC. Created RADH2 to contributed to complex II

Malate-asparate shuttle: cystolic oxalacetate, cannot pass through inner mitochondrial membrane and is reduced into malate, which can. Once malate crosses into matrix, mitochondrial malate dehydrogenase reverse the reaction to form mitochondrial NADH and pass electrons to complex I.

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99
Q

What is the difference between chemiosmotic and conformational coupling?

A
  1. Chemiosmotic: H+ flow into F0 protions of ATP synthase and chemical energy of gradient is harnessed to convert ADP into ATP in F1 portion
  2. conformational: proton gradients and ATP synthesis is indirect. ATP releases by synthase as a result of conformational changes caused by gradient (turbine)
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100
Q

How is cystein different from other amino acids?

A

It is in the R configuration while the rest of amino acids are in the S

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101
Q

How are peptide bonds formed and cleaved?

A

Formed by condensation reactions and cleaved by strong acids and based

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102
Q

Why is the C-N bond in an amide planar?

A

it is a partial double bond character due to resonance

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103
Q

What are the two ways amino acids are synthesized?

A
  1. Strecker synthesis
  2. Gabriel Synthesis
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104
Q

What are two characteristics that make inorganic phosphates have so much energy?

A
  1. contain negative charge, so when bonded to other phosphate groups, this creates repulsion with adjacent phosphate groups
  2. can be resonance stabilized
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105
Q

What is an organic phosphate?

A

are carbon containing compounds that also have phosphate groups (ATP,GTP, DNA)

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106
Q

What are two traits of phosphoric acids?

A
  1. three acidic hydrogens with unique pKa
  2. wide variety of pKa act as a moderate buffer over a large range of pH values. can pick up or donate H+
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107
Q

What 4 substances contributes to chemical digestion of lipids in small intestine?

A
  1. bile
  2. pacreatice lipase
  3. colipase
  4. cholesterol esterase
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108
Q

What is one difference between how large and small fatty acid chains are absorbed?

A
  1. Small: absorbed across intesting into blood
  2. long: are absorbed as micelles and assembled into chylomicrons for releases in lymphatic system
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109
Q

What are 3 traits of hormone-sensitive lipase (HSL)?

A
  1. insulin activates it/ also epinephrine and cortisol can activate it
  2. hydrolyzes triacylgerols, yeilding fatty acids and glycerol –> releases glycerols can go to liver for glycolysis or glucogenesis
  3. effective within adipose tissue
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110
Q

What are the 5 different types of lipoproteins? Function?

A
  1. Chylomicrons: transport triacylglycerols, cholesterol, and cholesteryl esters from intestine to tissue
  2. VLDL: transports triaglycerols and fatty acids from liver to tissue/ produced and assembled in liver cells
  3. IDL: picks up cholesteryl esters from HDL to become LDL
  4. LDL: delivers cholesterol into cells
  5. HDL: picks up cholesterol accumulating in blood vessesl/delivers cholesterol to liver and steroidogenic tissues/transfers apoliproteins to other lipoproteins. synthesized in liver and intestines
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111
Q

What are apoproteins?

A

they are receptor molecules and are involved in signaling/control interactions between lipoproteins

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112
Q

What is the primary method of transporting free fatty acids in blood?

A

free fatty acids remain in blood, bonding to albumin and other carrier proteins. Much smaller amount will remain unbonded

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113
Q

Order the 5 lipoproteins from greated percentage to least?

A

HDL>LDL>IDL>VLDL>chylomicrons

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114
Q

where are lipoproteins primarly synthesized?

A

liver and intestine

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115
Q

Where does fatty acid synthesis take place?

A

cytosol, mostly in liver

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116
Q

How do fatty acids enter mitrochondria for beta oxidation?

A

Small and medium sized chains can freely diffuse. Long chains need carnitine acyltransferase I (rate-limiting enzyme of oxidation)

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117
Q

What what are three product generated by beta oxidation?

A
  1. FAD–> FADH2
  2. (NAD+–> NADH)
  3. acetyl-CoA
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118
Q

what does acetyl-CoA stimulate in the liver?

A

glucogensis by activating pyruvate carboxylase

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119
Q

How does Beta oxidation of unsaturated fatty acids differ from that of saturated fatty acids?

A

additional isomerase and reducatasewhich provide the sterochemistry necessary for futher oxidation

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120
Q

What is ketogenesis? What is the main enzyme?

A

occurs in the mitochondria of liver cells when there is excess acetyl-CoA acculating during fasting

HMG-CoA synthase main enzyme

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121
Q

What is ketolysis?

A

aim to regain energy via oxidation of ketone bodies, which takes place in mitochondria. stimulated by low energy states in muscle and brain tissue

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122
Q

What is ketolysis of brain?

A

during prelonged fast, the brain gets 2/3 of its energy from ketone bodies are metabilized in acetyl-CoA.

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123
Q

Why are fatty acids used to create ketone bodies instead of creating glucose?

A

fatty acid degradation results in large amounts of acetyl-CoA, which cannot enter the gluconeogenic pathway to reproduce glucose. only odd numbered fatty acids can act as a source of carbon for gluconeogenesis

fatty acid synthesis is used to store energy

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124
Q

Where does proteolysis occurs and what enzymes are involveed?

A

Stomach: pepsin

small intestine: trypsin, chymotrypsin, carboxypeptidases A and B

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125
Q

How are proteins used for energy?

A

amino acids are released from proteins through transamination or deamination and carbon skeleton is used for energy

amino acids are fed into urea cycle in liver

126
Q

What can glucogenic and ketogenic amino acids be converted into?

A

Glucogenic(all but luecine and lysine) can be converted into glucose through gluconeogensis

ketogenic (leucine and lysine, isoluecine, phenylalanine, threaonine, tryptophan, and tyrosine) can be converted into acetyl-CoA and ketone bodies

longest carbon change–> most energy

127
Q

What is the only fatty acid humans can synthesize?

A

palmitic acid, which is fully saturated and contained 16 carbons and synthesized from 8 molecules of acetyl-CoA

128
Q

Where do the majority of triacylglcerols stores in adiposecytes come from?

A

liver

129
Q

Why is ATP an ineffecient molecule for long term energy storage?

A

The higher energy bonds in ATP and the presence of a significant charge make it an inefficient molecule to pack into a small space. long term energy sotrage molecules are dense and stable, nonrepulsive bonds

130
Q

What are three facts about flavoproteins? What are two examples?

A
  1. derived from vitamin B2 or riboflavin
  2. either in the form of FAD or FMN
  3. primarly in mitochondira and chloroplasts as e carriers
131
Q

What are three traits about the Postsprandial state (absorptive state)?

A
  1. occurs shortly after eating
  2. greater anabolism (synthesis of molecules) and fuel storage than catabolism (break down of molecules for energy)
  3. increase in insulin to promote glycogen formation in muscle and liver and triacylglycerol synthesis in adipose tissue.
132
Q

What five types of cells are insensitive or insulin

A
  1. nervouse tissue
  2. kidney tubules
  3. intestinal mucosa
  4. RBCs
  5. beta-cells of the pancreas
133
Q

What are three traits of the postabsorptuve (fasting) state?

A
  1. counterregulatory hormones increase (glucagon, cortisol, epinephrin, norepinephrine, GH)
  2. glycogenolysis increases
  3. release of amino acids from skeletal muslces and fatty acids from adipose tissues are stimulated by decrease in insulin and increase in epinephrine
134
Q

What are three traits of the prolonged fasting (Starvation) state?

A
  1. levels of glucagon and epinephrine are elevated
  2. liver glycogen storage is depleted
  3. lipolysis occurs to make ketone bodies
135
Q

Which tissue is least able to change its fuel source in periods of prolonged starvation?

A

cells that rely solely on anaerobic respiration are the least adaptable to different energy sources. RBCs are least flexible and rely on glucose

136
Q

What is one fact about insulin?

A
  1. increases rate of anabolic rxn such as (glycogen synthesis), increase amino acid uptake by muscle cells so increase protein synthesis, triacylglycerol synthesis
137
Q

What are 7 facts about glucagon?

A
  1. secretede by alpha cells in pancrease
  2. primary target are hepatocytes
  3. increases glycogenolysis/inactives glycogen synthase
  4. increase in gluconeogenesis
  5. increase liver ketogensis and decreases lipogensis
  6. increase lipolysis in liver and actives hormone sensitive lipase in liver
  7. increase release when higher basic amino acids in blood
138
Q

What are glucocorticoids and what is one example?

A
  1. increase blood glucose in response to stress by mobilizing fat stores and inhibiting glucose uptake. Increase the impact of glucogon and catecholamins
  2. cortisol increase lipolysis and amino acid mobilization, while decreasing glucose uptake in certain tissue and enhacing activity of counterregulatory hormones
139
Q

What are catecholamines and what are two examples?

A
  1. catecholamines are secreted by adrenal medulla/promote glycogenolysis and increase basal metabolic rate through their sympathetic nervouse system activity. increase lipolyisis by increasing activity of hormone sensitive lipase in adipose tissue
  2. epinephrine and norepinephrine
140
Q

What are thyroid hormones and what are two specific ones?

A
  1. modulate the impact of other metabolic hormones and have a direct impact on basal metabolic rate. main effect on lipid and carb metabolism
  2. T3 is more potent that T4
141
Q

When is hormone sensitive lipase released?

A

release in fat cells during fasting state to release fatty acids into circulation

142
Q

What is a very short lived source of energy in active muscle?

A

creatine phosphate, transfers a phosphate group to ADP to form ATP

143
Q

How is cardiac muscle different from skeletal muslce?

A

prefers fatty acids as their major fuel in both well fed anf fasting states

144
Q

How to skeletal muscle metabolism differ bases on activity?

A
  1. resting muscle conserved carbs in glycogen stores and uses free fatty acids from blood stream
  2. active muscle may use anaerobic metabolism, oxidative phosphorylation of glucose, creatine phosphate, fatty acid oxidation
145
Q

What organ consumes the greatest amount of glucose relative to percent of body mass?

A

brain

146
Q

What is the respiratory quotient? What does it measure? What are respiratory quoients of lipids, carbs?

A

RQ=(CO2 produced)/(O2 consumed)

composition of fuel thay is actively consumed by the body

lipid: 0.7
carbs: 1

147
Q

What three hormones influence appetite and how?

A
  1. Ghreline is secreted by stomach in response to signals of impendeing meal (sight, sound, taste smell). increases appetite and stimualted orexin
  2. Orexin: futher increases appetite, involved in alertness and sleep-wake cycle
  3. leptin is secreted by fat cells that decrease appetite by supressing orexin production
148
Q

What is the charge within a sodium channel?

A

+ because Na+

149
Q

What are two facts about disulfide bonds?

A
  1. they can only be between two cystein amino acids
  2. the formation involves oxidation of S and breaking involves reduction of S
150
Q

How do you find the isoelectric point of histadine with a pKa of 6?

A

Caboxylic acid has a pKa of 2, amino group has a pKa of 9. Since hsitadine is basic, use the two basic pKas

(9+6)/2

151
Q

What is the turnover number and how do you calculate it?

A
  1. kcat: it is the time it takes one enzyme to turnover a maximum amount of substrate molecules per unit time
  2. kcat=Vmax/[E]
152
Q

How do you find catalytic efficiency?

A

kcat/Km

153
Q

What is a coenzyme? Cofactor?

A

nonprotein/ organic compound necessary for function of enzyme. Coenzyme is a type of cofactor. cofactor can be organic or inorganic

154
Q

What is are prosthetic groups?

A

type of coenzymes tightly bound to enzyme

155
Q

Where does an uncompetitive inhibitor bind? How do Km and Vmax change?

A

Enzyme-substrate complez

both decrease

156
Q

What is vitamin B?

A

coenzyme, cofactor

157
Q

What is homotropic regulation?

A

molecule serves as a substrate and a regulatory molecule

158
Q

What is aconitase?

A

converts citrate into cis aconitate in citric acid cycle

159
Q

What is Mg the cofactor of?

A

glycolysis

160
Q

What is rate limiting step in citric acid cycle?

A

generation of a five carbon molecule

161
Q

Where is glucokinase located? what is it responsive to?

A
  1. liver and pancrease P cells
  2. responsive to insulin
162
Q

What are the 4 things PFK1 is inhibited by?

A

ATP, low Ph, PEP, citrate

163
Q

What are two difference between microtubules and microfilaments?

A
  1. actin filaments are assembled from monomeric units of actin. Microtubules are assembled by dimeric tubulin heterodimers
  2. GTP is used for Tubulin synthesis and ATP is used for actin synthesis
164
Q

How do actin filaments move?

A
  1. Myosin
165
Q

What is axoplasmic transport and what are the two motor proteins used?

A
  1. movement of membrane bound organelles
  2. Microtubules associated motor proteins:

Kinesin (antereograde transport: towards cell membrane)

Dyneisin (retorgrade transport: toward the center of cell)

166
Q

How many heavy chains and light chains in Ig?

A

two heavy chains and 2 light chains

167
Q

How are G protein decativates?

A

GTP hydrolysis

168
Q

What are carboxylases?

A

add carboxyls

169
Q

What are two characteristics of conjugated systems?

A
  1. alternating double and single bonds
  2. absorb UV light
170
Q

What are pyridine, imadazole, pyrrole?

A
  1. pyridine: 6 member ring with N
  2. imadazole: 5 member ring with O
  3. pyrrole: 5 member ring with -NH
171
Q

What is collagen compassed up?

A

triple helix formed by 3 proteins

they cross link with eachother in extracellular space

172
Q

Under what conditions with disulfide links break?

A

reducing conditions

173
Q

What is salting in? Salting out?

A
  1. Salting in: addition of salt to a solution, salt intercts with charged amino acids side chains, decreases protein’s ability to aggregate with other proteins so increase solubility
  2. salting out: when salt concentrations are high, protein solubility decreases
174
Q

What are the signs of anode and cathode in electrophoresis?

A

like an electrolytic cells so anode is + and cathode is -

175
Q

What drives fatty acid oxidation? Fatty acid synthesis?

A
  1. Higher NAD+ /NADH ratio will drive catabolism
  2. lower NAD+/NADH ratio will drive anabolism
176
Q

Where does fatty acid oxidation occur and how does it get there?

A

occurs in the mitochondria, following transport by carnitine shuttle via beta oxidation

177
Q

How is resting muscle different from active muscle and cardiac muscle?

A
  1. Resting muscle uses free fatty acids
  2. active muscle uses carbs, fatty acid oxidation
  3. cardiac muscle uses fatty acid oxidation
178
Q

What are Hormone sensitive lipases and where are they expressed?

A
  1. expressed in adipose tissue and adrenal cortex, ovaries, testies
  2. catelyze the breakdown of tracylglycerols and glycerol through hydrolysis of ester linkages
179
Q

What are three facts about Acyl-CoA dehydrogenase?

A
  1. enzymes involved in the first step of beta oxidation
  2. break down fatty acids in mitochondria–> broken down into ketone bodies when freely diffuse across the blood brain barrier, then converted into Acetyl CoA
  3. glucogenic amino acids can be converted into glucose during extended fasting
180
Q

How are LDLs different from chylomicrons and VLDL?

A

LDLs transport cholesterol to tissue and others transport triglycerols

181
Q

Where does glucokinase located and what is it responsive to?

A

In liver and pancreatic Beta cells

responsive to insulin

182
Q

How does cAMP cascade influence PFK2? Where does it happen?

A
  1. deactivates kinase functions which turns off PFK2 so glycolysis decreases
  2. happens in liver so gluconeogensis can occur, which is restricted to liver
  3. insulin activates protein phosphatase which depholsphorylates PFK2
183
Q

What is the pentose pathway? What is the Rate limiting enzyme?

A
  1. occurs in the cytoplasm in most cells generating NADH and sugars for biosynthesis
  2. G6P dehydrogenase is activated by NADP+ and insulin
184
Q

Where is palmitic produced and from where?

A

in cytoplasm from acetyl-CoA transported out of mitochondria

185
Q

How does miRNA alter expression?

A

single nucleotide strands incorporates into an RNA structure with a hairpin loop

186
Q

What are lysases?

A

cleave bonds through non-hydrolysis mech

187
Q

What does aldosterone do? Where does it work?

A
  1. Increase HB, [NA+], excreation of K+/H+
  2. works in convuluted tubule and collecting duct
188
Q

How does ADH work?

A

increase permeability of collecting duct

189
Q

How and where does ANP work?

A
  1. decrease BP, NA+ absorption/ inhibits aldosterons, increases glomerula filtration
  2. works in distal convuluted tubule and collecting duct
190
Q

What is the rate law of an enzyme that is completly saturated

A

zero-order

191
Q

During the introduction of a substrate to an enzyme, what rate law describes the rxn?

A

first-order

192
Q

What is beta oxidation?

A

fatty acids are broken down into acetyl-CoA and fed into citric acid cycle and generate NADH and FADH2

fatty acid is oxidized to CO2

193
Q

What is the pKa of carboxylic groups? amino groups?

A
  1. 2
  2. 9-10.5
194
Q

What is the function of NADPH?

A

important function in anabolic pathways such as lipid and nucleic acid synthesis

have more NADPH compared to NADP+ unlike NAD where have more NAD+ than NADH

195
Q

What is the function of transketolase in pentose pathway?

A

responsible for catalyzing the production of G3P and F6P to go into glycoylsis

196
Q

What are antisense strands?

A

complemenatary strand (form double stranded product, such as DNA)

197
Q

Is the anomeric carbon a reducing sugar?

A

yes, attached to two O

198
Q

What are the bonds in sucrose? fructose? maltose?

A
  1. Sucrose: glucose alpha 1,2 fructose
  2. Lactose: galactose beta 1,4 glucose
  3. Maltose: glucose beta 1,4 glucose
199
Q

What is 2 mecaptoethanol?

A

BME

reducing agent of disulfide bonds

200
Q

What are coenzymes?One Exp?

A

donate functional groups

ATP

201
Q

What is one inorganic and one organic cofactor?

A

Inorganic: metal oxides

Organic: ATP

202
Q

Does inhibition of enzyme inhibit overall rxn?

A

no

203
Q

What 4 compounds does the gluconeogenic pathway act on? What is the one compound it does not act upon?

A

pyruvate, lactate, glycerol, glucogenic amino acids

does not act on even-chain free fatty acids

204
Q

Where should you inhibit an enzymatic pathway to minimize side effects?

A

the last possible enzyme

205
Q

If protein is denatured, what bonds are left?

A

the covalent bonds between amino acids

206
Q

How can you detect the first mRNA strand in RT-PCR? (if the RNA primers do not have repeats)

A

with a poly T probe because will have a poly A tail that will not get copied

207
Q

What nucleotides are telomers made of?

A

G and C

208
Q

What is the difference between a thioester, thioether, and thioketon?

A
209
Q

What are three products of beta oxidation?

A

NADH, FADH, acetly CoA

210
Q

What are fatty aacid/cholesterol derivatives?

A

Terpenes/terpenoids (Repeating C5H8)

VDL/LDL/HDL/IDL

211
Q

What are two components of ATP?

A

pentose +Purine

212
Q

What 4 substanves produce free radicals?

A

FADH2, NADH, Vit E, Ubiquinone

213
Q

What is a calorie?

A

amount of heat required to raise temp of one gram of water by one degrees C

214
Q

How are cellulose and glycogen different?

A

Glycogen had alpha 1, 4 glycosidic lonks

cellulose has beta 1,4 glycosidic links

215
Q

Is glycogen more branched than amylopectin?

A

yes

216
Q

What type of hormone is ACTH?

A

peptide

217
Q

In TCL, what elute second?

A

polar

218
Q

What is the apoprotein?

A

unbound to prosthetic group(non protein component)

219
Q

What is the function of vitamin K?

A

coagulation

220
Q

What are the three usual endings of steroid hormone names?

A

-ol, -one, -en

221
Q

What is the role of vitamine C?

A

collagen

222
Q

What can a vitamin B deficiency lead to?

A

deficiency can lead to memory dysfunction (karsakoff) and cardiovascular problems

223
Q

Besides vision, what does vitamin A play a role in?

A

immune function and normal growth

224
Q

Are SnRNA, SnoRNA, and HnRNA non-coding or coding?

A

SnRNA and SnoRNA are non coding and play a role in RNA biogensis and modification of rRNA and tRNA (Found in nucleus)

hnRNA are precursor for mRNA so are coding –> do turn into protein

225
Q

Does lysine have a larger or smaller pKa compared to histadine?

A

larger

226
Q

What is the net ATP after glycoylsis? How many ATPs in investment steps?

A

2 ATPs

2 ATP (1ATP required to phosphorylate)

227
Q

What will build up when an aerobic organism is in a O2 poor environment?

A

bult up NADH+ because undergoing excessive glycolysis

228
Q

What happens when a protein cannot fold into secondary, teritary, and quatanary structures?

A

it will maximize its entropy

229
Q

What is the average weight of an amino acid?

A

110 Da

230
Q

If you want to maintain a tetromer or dimer configurations with anSDS page, should you denature and reduce?

A

no, just reduce

231
Q

What is another name for proteolytic cleavage?

A

hydrolysis rxn

232
Q

What is rate limiting step in gluconeogensis?

A

oxalacetate in mitochondira is converted to malate to export from mitochondria and then converted and rexoidized back into oxolacetate when in cytoplasm

233
Q

What is homotropic regulation?

A

molecules serves as a substrate and a regulatory molecule

234
Q

What is a lipase?

A

catalyzes the break down of fatty acids, glycerol, alcohols

235
Q

What is the difference btw ribose and fructose?

A
236
Q

What is nicotinamide?

A

NAD+

237
Q

What structure is this?

A

GTP

238
Q

What does an SDS page remove?

A

quatenary protein structures

239
Q

What is a glycoside bond?

A

links monosaccharides togethers in oligosaccharides

240
Q

What type of chromatography is histine tagging and nickel column?

A

affinity chromatography

241
Q

What does GADPH catalyze?

A

the reversible conversion of G3P to 1,3 biphosphoglycerate

242
Q

What mediates the internalization of viral particled through endocytosis?

A

endosomes

243
Q

Where do microtubules orginate from?

A

centrosomes

244
Q

What is deamination? which amino acids can undergo deamination?

A

the removal of an amide group (asparagine and glutamine)

245
Q

What are the three differences between a noncompetitive and an uncompetitive inhibitor?

A
  1. uncompetitive inhibitors bind to enzyme-substrate complex only(need substate to bind) but noncompetitive bind to enzyme and enzyme-substrate complex)
  2. for noncompetitive inhibitors Vmax decreases and Km stays the same, but for uncompetitive both Km and Vmax decrease
246
Q

What does a Hill coffecient of 1 mean?

A

not cooperative

247
Q

What are five important steps in krebs cycle?

A
  1. D-isocitrate–> alpha ketoglutarate creates NADH
  2. Alpha Ketoglutarate to succinyl-Coa create NADH
  3. Sucinyl-Coa to Succitate create GTP
  4. Succinate to Fumerate creates FADH2
  5. Malate to oxaloacetate creates NADH
248
Q

What is one enzyme that catalyzes both gluconeogenisis and glycogenolysis?

A

glucose 6 phosphatase

249
Q

What is Kcat used to describe?

A

used to describe the rate limiting step of catalysis under staturating conditions of substrate

250
Q

How many H-bond donors and acceptors in A, T, G, C?

A

A: 1 donor, 1 acceptor

T: 1 donor, 1 acceptor

G: 2 donors and 1 acceptor

C: 1 donor and 2 acceptors

251
Q

What are three things that affect thermal denaturation?

A
  1. pH of solution
  2. Ionoic strength of Solution
  3. length of DNA strand
252
Q

What type of phosphate is involved in phosphoryl tranfers from kinases?

A

gamma phosphate in ATP

253
Q

What is a dehydrogenase?

A

remove H to form a double bond (oxireducatate)

254
Q

Where is phosphoglucose isomerase inolved?

A

glycolysis

255
Q

Do neutral side chains of amino acids influence pKa?

A

no

256
Q

What is the size of prokaryotic and a eukaryotic ribosome?

A

70s/80s

257
Q

What does monocistronic mean?polycistronic?

A

monocistronic: when mRNA contains a coding sequence for a single protein (eukaryotes)
polycistronic: Carry many ORFs and each is coded into a protein, they are regulated by a single promoter and operator

258
Q

What type of primers does PCR use?

A

DNA

259
Q

How do you find association constant of enzyme? Dissociation constant?

A

[Es]/([E]x[S])

inverse

260
Q

What is photoreactivation? What do eukayrotics use in replacement?

A

a prokaryotic process to reverse the damage done by UV light. Base exicision repair (prokaryotics can use this too)

261
Q

What is oposonization?

A

antibodies bind to and recognize antigens on the surface of a pathogen. these antibodies then attrack macrophages

262
Q

do macrophages release cytokines?

A

yes

263
Q

What is the difference between amphoteric and amphipathic?

A

Amphoteric: able to act as an acid or base/ amphipathic: both hydrophilic and hydrophobic

264
Q

What vitamins are fat soluble?

A

vitamin BEAK

265
Q

What is/are the most electrons exchnages in ETC?

A

1

266
Q

Do type two diabetics have higher or lower than normal insulin?

A

higher than normal because not responsive to insuline, bllod sugar is not lowering

267
Q

Can reversible reactions be committed steps?

A

no

268
Q

Where does fatty acid catabolism (beta oxidation) occur and then end?

A

start in cytosol and end in mitochondria

269
Q

What is the difference between beta oxidation and cell rep?

A

The cell requires more than twice the number of NAD+ electron carriers compared to FAD electron carriers, in order to harvest ATP from fatty acids

270
Q

What happens to lipolysis when eat?

A

decreases

271
Q

What reducing agent aids in glutathione reduction?

A

NADPH as it relieves oxidative stress by aiding in the conversion of hydrogen peroxide to water

272
Q

What are two hormones that can increase gluconeogensis?

A

glucagon and norepinephrine

273
Q

What are three things the pentose pathway produces?

A

G3P, NADPH, and nucleic acids

274
Q

What is the difference between allosteric modulators and inhibitors?

A

modulators change the affinity but inhibitors change V max

275
Q

How would an alloesteric modulators impact kinetics of a rxn?

A

allosteric activation would increase the initial rate and allosteric inhibition will decrease the initial rate but for both the Vmax will stau the same

276
Q

What are two water soluble vitamins?

A

B (coenzyme, prosthetic group) and C (antioxidant)

277
Q

What is a Carotenoids?

A

vitamin A

278
Q

What are the two difference between hexokinase and glucokinase?

A

Hexokinase has a higher affinity for glucokinase. Glucokinase works in pancreas and liver

279
Q

How many carbons in acetly Coa?

A

two

280
Q

Do HDLs or LDLs contain more cholesterol?

A

LDLs

281
Q

What is the purpose of glycosyltransferase enzym?

A

intiation and longation of glycogen

282
Q

What is glycogen phosphorylase?

A

release glucose from alpha 1,4 linkages and is rate limiting step

283
Q

What does two rounds of ATP hydrolysis lead to?

A

AMP

284
Q

What enzyme is required to make GTP?

A

Nucleoside diphosphate kinase

285
Q

What is a ketone body you can smell from one’s breath?

A

acetone

286
Q

Does an enzyme reduce the activation for both the forward and reverse rxn?

A

yes, The direction of reaction in this case is governed by the relative amounts of reactants and products, i.e. the difference between the reaction quotient and equilibrium

287
Q

What are the two ways a competetive inhibitor acts?

A

can simulate substrate and also the transition state because enzymes have a strong affinity for the transition state

288
Q

What is the role of transketolase?

A

involved in non-oxidative step in pentose pathway to produce G3P and F6P

289
Q

Do enzymes that display cooperative binding display michaelis-menten kinetics?

A

no

290
Q

What hormone stimulates fatty acid oxidation? What does fatty oxidation fuel?

A

glucagon

gluconeogenesis

291
Q

What type of carbon chain has the most energy?

A

longest and most saturated

292
Q

How many NADHs, FADHs and GTPs are created from acetyl CoA?

A

3NADH, 1 FADH, 1GTP

293
Q

What is the first molecule involved in pentose phosphate pathway?

A

G6P

294
Q

What is the difference between allosteric activation and allosteric inhibitor?

A

Allosteric inhibition: slow the initial rate but same Vmax

Allosteric activation: increase initial rate but same Vmax

295
Q

What is the shape of graph of alloesteric enzyme?

A

sigmoidal

296
Q

Does Vmax change if add mor enzyme?

A

yes

297
Q

Compare coenzyme and prosthetic groups?

A

are cofactos but prosthetic groups bind to enxyme

coezymes released from active site (NADH)

298
Q

What are three substances gluconeogenesis can directly use?

A

pyruvate, glycerol, lactate

299
Q

How is lactate converted into pyruvate?

A

through the cori cycle

300
Q

Where do phosphates come from and inorganic phosphates?

A

ATP: phosphates

NADH: inorganic phosphates

301
Q

What is catabolism?

A

breakdown

302
Q

What is hormone sensitive lipase?

A

breakdown into fatty acids

303
Q

How to transferases work with glycogen?

A

tak a segment of the branched chain that is one unit away from the branch point and relocated it to parent chain

304
Q

What do you need for fatty acid synthesis?

A

acetly CoA and NADPH

305
Q

What happens during starvation?

A

decrease pentose phosphate pathway bc was G6P

306
Q

What is AMP?

A

low energy state

307
Q

What are 4 types of nucleotides?

A

cAMP, GTP, ATP, cGMP

308
Q

What does pyruvate dehydrogenase do?

A

convert pyruvate into acetly CoA

309
Q

What is a coenzyme of hemoglobin?

A

iron (dissociate after rxn, can transfer functional groups)

310
Q

Where does gluconegensis occur?

A

kidney and lover

Amanda's MCAT Flashcards (6 decks)

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