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Catalytic Site Atlas

CSA LITERATURE entry for 1guf

E.C. nameenoyl-[acyl-carrier-protein] reductase (NADPH, B-specific)
SpeciesCandida tropicalis (Yeast)
E.C. Number (IntEnz) 1.3.1.10
CSA Homologues of 1gufThere are 133 Homologs
CSA Entries With UniProtID Q8WZM3
CSA Entries With EC Number 1.3.1.10
PDBe Entry 1guf
PDBSum Entry 1guf
MACiE Entry 1guf

Literature Report

Introduction2-enoyl thioester reductases catalyse the reduction of trans-2-enoyl acyl carrier protein/coenzyme A to acyl carrier protein/coenzyme A. Yeast enzymes, such as Etr1p and Mrf1p, are responsible for the NADPH dependent reaction in mitochondrial fatty acid synthesis, and are indispensible for respiratory function in yeast. They belong to the medium chain dehydrogenases/reductases (MDR) superfamily and are structurally distinguishable from the prokaryotic 2-enoyl thioester which belong to the short chain dehydrogenases/reductases (SDR) superfamily.
MechansimBy analogy with the prokaryotic enoyl thioester reductases, hydride is transferred from NADPH to the beta position of the alpha-beta unsaturated carbonyl substrate (Michael addition) to give an enol(ate) intermediate. The hydroxy group of Tyr 79 acts as an electrophilic catalyst by forming a hydrogen bond to the substrate carbonyl to stabilise the intermediate and the transition state leading to it.
Reaction

Catalytic Sites for 1guf

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrA7979macie:sideChainHydroxyl group acts as an electrophilic catalyst, forming a hydrogen bond to the carbonyl of the substrate to stabilise the transition state.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrB7979macie:sideChainHydroxyl group acts as an electrophilic catalyst, forming a hydrogen bond to the carbonyl of the substrate to stabilise the transition state.

Literature References

Notes:1. The Candida tropicalis genes ETR1 and ETR2 both encode enzymatically active 2-enoyl thioester reductases, which can form both homodimers and heterodimers. 2. The proposed mechanism is based on analogy with the prokaryotic enoyl thioester reductases such as InhA. The yeast enzymes are structurally distinct from those of prokaryotes, belonging to the medium chain dehydrogenases/reductases (MDR) superfamily rather than the short chain dehydrogenases/reductases (SDR) superfamily. However, both classes contain an appropriately positioned tyrosine residue that is essential for catalysis.
Airenne TT
Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance.
J Mol Biol 2003 327 47-59
PubMed: 12614607
Parikh S
Roles of tyrosine 158 and lysine 165 in the catalytic mechanism of InhA, the enoyl-ACP reductase from Mycobacterium tuberculosis.
Biochemistry 1999 38 13623-13634
PubMed: 10521269
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