1- Fundamentals Of Biochem Flashcards Preview

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Flashcards in 1- Fundamentals Of Biochem Deck (16):
1

Cofactors

Metal ions, essential trace elements, interact with enzyme via noncovalent interaction, stabilize active site

2

Coenzymes

Small organic molecules, derived from vitamins

3

Cytochrome c oxidase

Cu COFACTOR
Accepts electrons from cytochrome-c in the electron transport chain

4

Superoxide dimutase

Cu COFACTOR
Antioxidant
Binds the free radical of molecular oxygen

5

Heme proteins (hemoglobin and myoglobin)

Fe COFACTOR
- require FE2+ to bind O2

6

ATPases

Mg COFACTOR
Hydrolyze ATP to ADP and use the released energy to do mechanical work like transport ions

7

Gluthanthione peroxidase

Se COFACTOR
Antioxidant, detoxifies hydrogen peroxide

8

Superoxide dismutase

Zn COFACTOR
(Antioxidant)
Binds the free radical of molecular oxygen

9

Coenzyme 2 subdivisions

1) co-substrate: temporary association (bind then detach in altered state)
- I.e. NAD+
2) prosthetic: permanent association
- I.e. Heme, FAD

10

Carbonic anhydrase

Zn COFACTOR
inter converts CO2 and bicarbonate to balance blood pH

11

competitive inhibition

Vmax no change
Km increases
- compete for binding site with substrate

12

noncompetitive inhibition

Vmax decrease
Km increases
- binds to E and ES complex, at site other than substrate active site

13

uncompetitive inhibition

Vmax decreases
Km decreases (by same factor//parallel line)
-only binds to ED complex at site other than substrate binding site

14

allosteric enzymes

- activity modulated by noncovalent binding of a metabolite to a site other than the catalytic site
- affects substrate by inducing conformational changes with binding
- can be POSITIVE (activators) or NEGATIVE (inhibitors) effectors

15

isozyme and example

same catalytic function, different primary sequence

Example: markers of MI: Troponin cTn-1

16

proenzymes

inactive precursor of enzyme, cleavage of specific peptide bond generates the active form, made to be used in the future