184.108.40.206 - Pyruvate synthase
- Pyruvate synthetase.
- Pyruvic-ferredoxin oxidoreductase.
- 2-oxobutyrate synthase.
- 2-oxobutyrate-ferredoxin oxidoreductase.
- Alpha-ketobutyrate-ferredoxin oxidoreductase.
- Alpha-ketobutyrate synthase.
- Pyruvate oxidoreductase.
CoA + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate = acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Iron-sulfur; Thiamine diphosphate.
|AA||Uniprot||Uniprot Resid||PDB||PDB Resid|
overall product formed, proton transfer, assisted tautomerisation (not keto-enol), native state of cofactor regenerated, intermediate formation, colligation, electron relay, cofactor used, redox reaction, homolysis, intermediate terminated, native state of enzyme regenerated, decarboxylation, intermediate collapse, radical formation, hydride transfer, overall reactant used, inferred reaction step, unimolecular elimination by the conjugate base, bimolecular nucleophilic addition, tautomerisation (not keto-enol)
Glu64 deprotonates the thiamine diphosphate cofactor, which initiates double bond rearrangement that results in the deprotonation of the N=CH-S group, activating the cofactor.
The cofactor adopts the V configuration that brings the 4 imino group of the aminopyrimidine ring close to the C2 carbon of the thiazolium ring [PMID:16472741]. Hydrogen bonding of the carboxylate group from Glu64 to N1' of the aminopyrimidine ring increases the basic nature of the 4' position by generating the 4'-imino tautomer [PMID:11752578]. Binding of the substrate triggers the proton transfers [PMID10048931]. The mechanism shown here is supported by crystallographic studies [PMID:16472741].
The covalently bound pyruvate undergoes decarboxylation, resulting in double bond rearrangement, a single electron being transferred to ferredoxin via three iron-sulfur clusters and the formation of a one-electron bond between the cofactor and the formyl group.
The carbon dioxide reaction product remains tightly bound in the active site, consistent with the reversibility of the reaction [PMID:16472741]. The C2alpha-C2 bond between the acetyl and thiazole moieties is a one-electron unusually long bond PMID:11752578,PMID:16472741] and thus incompatible with enamine formation as postulated for a standard pyruvate decarboxylation cycle [PMID:16472741]. The generated intermediate shown here is supported by crystallographic studies [PMID:16472741].
There are no kinetic parameters information for this Enzyme
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