BCH 100 Final Prep Flashcards

(66 cards)

1
Q

What are Nucleotides for?

A

-Signaling
-Carrying Chemical Energy
-Cofactor Components
-Building blocks for Nucleic Acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Why do we need Amino Acids?

A

Precursor for proteins, Biomolecules and energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

How is an Amino acid catabolized?, What is the enzyme?

A

The amine group is removed by an -ketoglutarate to become glutamate and an -keto acid, Aminotransferase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Why are Glutamine and Alanine necessary in the blood?

A

They carry toxic amine groups through the blood to the liver to be excreted

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Draw Urea

A

H2N-(C=O)-NH2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Why does the Urea cycle happen and where does it occur?

A

The detoxification and exretion of excess NH4+, in the liver

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Write the Urea Cycle

A

Week 10 Lec 24

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Name the Essential Amino acids

A

Valine
Leucine
Isoleucine
Histidine
Lysine
Methionine
Threonine
Tryptophan
Phenylalanine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What are the two major ways Nitrogen is incorporated into the food chain?

A

Nitrogen-fixing bacteria converting atmospheric Ns to NH4+, Nitrogen-assimilating Plants and Bacteria conveting NO3- to NO2- to NH4+

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is Negative nitrogen balance?

A

If you are missing even one essential amino acid your body will keep eating through the protiens you have trying to find it, and you end up with such a large increase in Urea that you have more nitrogen leaving than coming in

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What is a Hormone?

A

an intercellular Chemical Messenger produced in the ductless glands of the endocrine system

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Name four hormones types and give examples

A

Steroids: estrogen, androgens
Polypeptides: insulin, glucagon
Amino acid derivitiives: Epinephrine (adrenaline)
Fatty acid derivatives: Prostaglandis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What are the three different hormone systems?

A

Endocrine (travel through blood)
Paracrine (travel to nearby cells)
Autocrine( targets the same cell)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

How do Hormones function?

A

They bind to a specific receptor on or in the target cell membrane, triggering a signal cascade that can alter enzyme activity or alter gene transcription

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What are the three major classes of membrane receptors?

A

7-Transmembrane a.k.a. G-protien coupled receptors
Dimeric membrane recepters that recruit protien kinases
Dimeric protien receptors that ARE protien kinases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Explain a GPCR cascade of Epinephrine

A

-Ep binds to the beta-adrenergic receptor -
-on the other side of the receptor in the membrane a G protien exchanges a GDP for a GTP and an alpha G dissociates from a betagamma G.
-Alpha G-GTP activates adenylate cyclase which converts ATP to cyclic AMP (cAMP), which is the second messenger that activates protein kinase A

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

How is GPCR regulated?

A

-Reciprocal regulation
-Active glycogen breakdown
-inactive glycogen synthesis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

How is the signal cascade stopped?

A
  1. No more signal
  2. Break down of cAMP, hydrolyzed by cyclic nucleotide phosphodiesterase back into AMP
  3. a built in timing mechanism of GTP on alpha G slowly hydrolyzing to GDP
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

How is RTK activated?

A

Binding to an RTK receptor causes it to autophosphorylate its own tyrosine residues, phosphotyrosines allow binding and phosphorylation of the receptor substrate causing a cascade

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

How is RTK regulated?

A

-stopping the hormone signal
-Removal of phosphates from activated proteins,

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Describe Glucagon

A

-29-amino acid polypeptide hormone
-Released by alpha-cells of islets of langerhans in the pancreas
-Signal for low blood sugar (starvation state)
-Binds to GPCRs on liver cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Describe Epinephrine

A

-Derived from Tyrosine in adrenal medulla
-Fight or flight hormone
-Acts on GPCRs of the liver and muscle cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Describe Insulin

A

-Peptide hormone
-Released by beta-cells of islets of langerhans (pancreas)
-Signal for high blood glucose (“fed” state)
made as preproinsulin, undergoes proteolytic cleavage
-chains held together by disulfide bonds
-Binds to RTK (NOT GPCR)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Describe a lipoprotien and its functions

A

Lipoprotiens transport TAGs and Cholesteral in the blood. The protein part solubilized lipids and direct the particle, the lipid parts are the fats that need to be transported

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
What are the categories of Lipoprotiens?
Chylomicrons: dietary fat (TAG) transport VLDL: very low density endogenous fat (TAG) transport LDL: low density, major cholesterol carrier in blood HDL: high density: reverse cholesterol transport
26
Why does the oxidation of fats yield more energy that oxidation of carbs?
Fatty acids are highly reduced
27
What are the ways and locations triacylglycerol used?
When broken down into glycerol: -it can enter the liver to go through glycolysis and become pyruvate or gluconeogenesis to become glucose. When broken into a fatty acid: it enters other tissues to go through beta oxidation and the citric acid cycle
28
Draw the beta oxidation cycle
Week 9 lec 21-22
29
How many NADH, FADH and GTP is made per cycle of Beta oxidation?
1NADH, 1 FADH
30
How many ATP per NADH and FADH?
2.5 NADH, 1.5 FADH
31
Where are ketone bodies made and under what circumstances?
Liver Mitochondria, ketosis happens High fat intake, low sugar, starvation and diabetes
32
Name 3 ketone bodies
-Acetoacetate -Acetone -Beta hydroxybutyrate
33
Name the 12, 14, 16, and 18 carbon fatty acids
12-Laurate 14-Myristate 16-Palmitate 18-Stearate
34
What is a lipid?
An organic molecule that is not soluble in water, but is soluble in organic solvents
35
What are the 5 main classes of fatty acid and their purposes?
1. Free fatty acids: Fuel 2. Triacylglycerols: Storage or fatty acids 3. Phospholipids: Membrane lipids 4. Glycolipids: membrane partly made of carbohydrates 5. Steroids: polycylic hydrocarbons with a variety of functions
36
How and where is fatty acid activated?
Fatty acid is activated by acyl-CoA synthase and occurs in the cytoplasm
37
How does activated fatty acid get into the mitochondria and what are the steps?
The carnitine shuttle transports fatty acid into the mitochondria: 1. carnitine acyltransferase -1 (CAT-1) transfers acyl to the carnitine 2. Carnitine translocase carries acylcarnitine into the matrix 3. CAT-2: transfers acyl from carnitine to CoASH to regenerate Acyl-CoA
38
Draw The Calvin Cycle
Week 8 lec 19
39
Define Photosynthesis
Using light energy to biosynthesize sugar
40
Draw the light dependent photosystem
Week 8 lec 19 (lower part)
41
Draw the electron transport chain
Week 7 lec 18
42
Whats the difference between a Nucleosides and Nucleotides?
Nucleosides: Base + sugar Nucleotides: Base + sugar + Phosphate
43
Whats the difference between Purines and Pyrimidines?
Purines: Two heterocyclic rings Pyrimidines: one Heterocyclic ring
44
Name the Purines
Purine, adenine, and Guanine
45
Name the Pyrimidines
Pyrimidine, Cytosine, Uracil, Thymine
46
What are the differences between purine and pyrimidine biosynthesis?
Purine synthesis: Start with sugar, build ring on ie Pyrimidine synthesis: Build base ring, add sugar
47
What are the two way to make nucleotides?
-Salvage pathways where you recycle nucleoside -De Novo synthesis where you make them from scratch
48
What is the committed step of Pyrimidine synthesis
Aspartate Transcarbamoylase
49
What is the committed step of Purine Synthesis
PRPP-gln amidotransferase
50
Draw Orotate
6 atom ring: 1N,2C,3N,4-6C
51
Draw Glycine
Amino acid slide
52
What do enzymes change and not change?
They change delta-G double dagger, the transition energy also known as the activation energy. They do NOT change delta-G (also written delta-g rxn), the reaction energy
53
On a reaction rate graph, what do the following mean? V0 Vmax K m K cat
V0: initial velocity Vmax: Maximum Velocity K m: Substrate concentration at 1/2 Vmax K cat: turnover number
54
On a Lineweaver-Burk graph what are: X axis: Y axis: X-intercept: Y-intercept: Slope:
X axis: 1/[S] Y axis: 1/V0 X-intercept: -1/Km Y-intercept:1/Vmax Slope: Km/Vmax
55
How do the three types of inhibitors affect the Lineweaver-Burk graphs?
Competitive shift slope but keeps y-intercept Uncompetitive shifts the intercepts but not the slope Noncompetititve shifts the slope but not the x-intercept
56
What naming monosaccharides, what does D and L mean?
From the last carbon, is the nearest alcohol up the chain to the right (D), or the left (L)
57
whats the name of a 5-ring sugar and a 6 ring sugar?
5: Furanose 6:Pyranose
58
How are Oligosaccharides connected?
O-glycosidic bonds
59
Define Maltose structure
Two cyclic glucose connected by a alpha(1,4) bonds
60
Define Lactose Structure
cyclic Galactos and cyclic glucose connected by beta(1,4) bond
61
Define Sucrose structure
Cyclic glucose and cyclic fructose connected by alpha(1,2) bond
62
Draw Fructose
Sugar structure handout
63
Draw Galactose
Amino Structure handout
64
What is the order for Purine nucleotide synthesis?
-PRPP synthetase -Glutamine-PRPP amidotransferase -Inosinate Formation -Ribonucleotide Reductase
65
Draw Succinate
COO- _CH2_CH2_COO-
66
Draw Pyruvate
COO-_C=O_CH3