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CO2
H2O
II. Coenzymes
Cosubstrates- altered in a reaction and dissociated from active site
- regenerated to original structure in a subsequent reaction
- transfer chemical groups among different enzyme reaction.
Prosthetic groups- remains bound to enzyme
- must return to original form
Both cosubstrates and prosthetic groups supply reactive groups not
present on the active site amino acid side chains
Vitamin derived coenzymes
ATP + substrate
SubstrateP
+ ADP
ATP + substrate
SubstratePP + AMP
ATP + substrate
SubstrateAMP + PPi
B. S-Adenosylmethionine (SAM):
Methionine + ATP
SAM
Methyl
group
Formation of UDP-glucose:
Glucosyl group
Nicotinamide coenzymes
Nicotinamide adenine dinucleotide (phosphate)
Precursor nicotinic acid (Niacin, B3)
Tryptophan can be degraded to niacin
Oxidation-reduction reactions
Flavin coenzymes
Flavin adenine dinucleotide (FAD); Flavin mononucleotide (FMN)
Precursor riboflavin (B2)
Prosthetic group
Oxidation-reduction reactions
FAD
Riboflavin
= H in
FMN
Co-enzyme A
Vitamin B5
ACP
TDP in decarboxylation
of pyruvate to
acetylaldehyde:
7. Biotin
-
Vitmain B3
Carboxyl group transfer reaction
ATP-dependent carboxylation
Prosthetic group
Bound to lysine residue in enzyme
8. Tetrahydrofolate (THF)
One-carbon
derivatives of
THF:
Cobalamin coenzymes
- Participate in reactions involving intramolecular rearrangements, methyl
group transfer, etc.
1. Intramolecular rearrangement:
5-methylTHF
THF
Cobalamin
Methylcobalamin
Methionine
Homocysteine