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Foundations Of Medicine PoNF > Biochemistry > Flashcards

Biochemistry Flashcards

1
Q

Functions of the citric acid cycle

A
  • Common metabolic pathway for all “fuel” molecules
  • fields energy that is passed to the etc which produces large amounts of ATP
  • it is efficient as it is cyclical and can make a lot of NADH + FADH2
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2
Q

Where does the Krebs cycle occur?

A
  • In the mitochondrial matrix
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3
Q

How is acetylcoA made

A

From pyruvate through action of enzyme private dehydrogenase

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4
Q

Can I keep selling sex for money officer?

A

Citrate
Isocitrate
A-ketoglutarate
Succinyl coA
Succinate
Fumarase
Malate
Oxoaloacetate

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5
Q

Function of glycogen in skeletal muscle and liver

A
  • 90% in liver + skeletal muscle:
    ~ liver: acts to replenish blood glucose when fasting
    ~ skeletal muscle: catabolism produces ATP for contraction
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6
Q

What reactions in the citric cycle involve electron carriers?

A
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7
Q

What steps involve the release of coz?

A

Oxidative decarboxylation

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8
Q

What are the classes of amino acids?

A
  • Aliphatic amino acids: ‘R’ group consists of hydrocarbon chains
  • aromatic amino acids: ‘R’ group consisting of hydrocarbon ring
  • Sulphur-containing amino acids: can make disulfide bridges to increase strength
  • basic amino acids
  • acidic amino acids: COO
  • polar amino acids: CH2OH
  • A miscellaneous amino Acid
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9
Q

Function of proteins

A
  • amino acids arranged in a particular structure that enables it to carry out a specific function in a particular context

-Structural: acts as a ‘scaffold’

  • functional: e.g. Enzymes/antibodies
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10
Q

Primary structure of proteins

A
  • Sequence of amino acid monomers bonded to form a polypeptide chain
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11
Q

Name for multiple monomers joined together

A
  • 2: dipeptide
  • 3: tripeptide
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12
Q

Secondary structure of proteins

A
  • The 3D spatial arrangement of amino acids, relies on hydrogen bonding between the amino acid hydrogen + carbonyl group of another amino acid in the chain
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13
Q

Tertiary structure of proteins

A
  • The ‘p’ chains of amino aceas in polypeptide chains interact with one another
  • Van der Walls, ionic, hydrogen, disulphide + hydrophobic interactions
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14
Q

Quaternary structure of proteins

A
  • Several polypeptides interacting to form a highly folded structure
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15
Q

What are the functions of proteins:

A
  • Structural
  • enzymatic
  • receptor
  • hormonal
  • Transport
  • storage
  • defensive
  • contractile
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16
Q

What properties would quaternary structure confer?

A
  1. Glycoproteins
  2. Lipoproteins
  3. Metalloproteins
17
Q

What are glycoproteins and what effect do they have?

A
  • Proteins with >1 carbohydrate molecule covalently attached
    1. Stability
    2. Solubility
    3. Cell signalling
    4. Orientation
18
Q

Lipoproteins

A
  • Proteins combine with lipids to form lipoproteins
  • found in cell membrane to transport hydrophobic molecules
19
Q

Function of metalloproteins

A
  • Protein molecule with metal ions in their structure
  • various functions: enzymatic, signal transduction,
20
Q

Globular vs fibrous proteins

A
  • Globular: storage, enzymes, hormones, transporters, structural
  • fibrous: muscle fibres t connective tissue
21
Q

How do enzymes lower activation energy?

A
  • Entropy reduction: orientate substrates in high ‘ direction so they bind and allow reaction to proceed,
  • desolation: weak bonds are replaced by by dragon bonds between substrate + aqueous solution
  • induced fit
22
Q

Ways reaction would vary if there was a change in concentration of enzyme or substrate

A
23
Q

What is the michaelis-menton plot + equation?

A
  • Assess how well a reaction is going (see notes)
24
Q

What does Km tell us?

A
  • A low valve = good fit

A high value = poor fit (takes a lot of substrate to get to 1/2 max

25
Q

What does V max tell us

A
  • How fast the reaction is proceeding when the enzyme is saturated with substrate.
26
Q

Competitive inhibition

A
  • Inhibitor binds to active site
  • vmax is unchanged
  • km increases because it takes more substrate to overcome inhibition
27
Q

Non competitive

A
  • Binds to secondary site & change shape of active site
  • V max decreased
  • km remains
28
Q

Why are enzymes measured in a clinical setting?

A
  • Detection of suspected disease at pre-clinical stage
  • confirmation of suspected disease and assessing severity
  • detecting of vitamin diseases etc.
29
Q

What factors can influence enzyme activity in a samples?

A
  • Age ‘
    -Gender
  • pregnancy
  • Drugs
  • time of day
  • genetics
  • race
30
Q

How is the release of enzymes from cells triggered?

A
  • Hypoxia: loss of oxygen supply
  • cellular damage: chemicals/ drugs
  • physical damage
  • immune disorder
  • genetic defeats
  • microbiological agents: bacteria, virus, forgi
  • nutritional disorders
31
Q

What are the tissue sources of serum enzymes?

A
  • Heart muscle; AST, LDH, ck -mb
  • liver/biliary track: AST, alt, got, alp
    Finish
32
Q

What are the main nitrogen containing molecules in the body?

A

Dietary Protein Camino acids, RNA +dwa)

33
Q

What is the fate of dietary protein?

A
  • enzymatically hydrolysed:
  • pepsin cuts protein into peptides in the stomach
  • trypsin and chymotrypsin cut proteins and larger peptides into smaller peptides in the small intestine
  • aminopeptides and carboxypeptides A and B degrade proteins into amino acids in the small intestine
34
Q

What is the role of glutamine in the + transfer of nitrogen, from and between amino acids?

A

Glutamate is the only amino- acid that can obtain its nitrogen directly from ammonium ions. Nitrogen from turned-over body protein is transported through plasma to liver as glutamine, or, from skeletal muscle, as alanine.

35
Q

Catabolism of dietary protein

A
  1. HC1 denatures protein in stomach
  2. Pepsin breaks it into ogliopepticle chains
    3.in the duodenum - digestive enzymes break into tri/di peptide and amino acids
    4.in the intestinal cells they all break down into amino acids
  3. Some stay but others go into bloodstream to different locations
36
Q

PKU

A
  • Cannot convert phenyculaline to tyrosine
    Brain impairment
37
Q

Formation of urea

A
  • Since ammonia (produced by krebscycle) is toxic it is converted to urea so we can excrete it softly

-In mitochondria: carbon dioxide and ammonium produces carbonyl phosphate

  • In cytoplasm:ornithine + carbonyl phosphate = citruline
  • citruline combines with aspartate = argino- succinate
  • argino-succinASE acts on argino- succinate= arginine and (fumarate)
  • arginate acts on arginine = UREA and ornithine (cycle begins again)
38
Q

Examples of metabolic defects in the urea cycycle give rise to clinical defects

A
  • Ornithine transcarbomylase (OTC) deficiency
    (Elevated blood amonia) (hyper ammonaemia)
39
Q

Types of enzymes (6)

A

Oxidorecductases: removes electrons

Transferases: group transfer

Lysases: transfer groups to carbon to carbon double bonds

Hydrolases: hydrolysis

Ligases: form carbon to carbon single bonds

Isomers: transfer groups to make isomers

Foundations Of Medicine PoNF (8 decks)

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