IUBMB Enzyme Nomenclature

EC 1.2.8.1

Accepted name: pyruvate synthase (flavodoxin)

Reaction: pyruvate + CoA + flavodoxin = acetyl-CoA + CO2 + reduced flavodoxin

Other name(s): pyruvate oxidoreductase (ambiguous); pyruvate synthetase (ambiguous); pyruvate:flavodoxin oxidoreductase; pyruvic-flavodoxin oxidoreductase

Systematic name: pyruvate:flavodoxin 2-oxidoreductase (CoA-acetylating)

Comments: The enzyme, found in some bacteria, uses the flavin mononucleotide (FMN)-containing protein flavodoxin as an electron donor under high-oxygen and low iron conditions. In some organisms ferredoxin may replace flavodoxin [cf. EC 1.2.7.1, pyruvate synthase (ferredoxin)]. The reaction is freely reversible. Reduced flavodoxin formed by the enzyme can serve as an electron donor for several enzymes, such as EC 1.19.6.1, nitrogenase (flavodoxin).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Shah, V.K., Stacey, G. and Brill, W.J. Electron transport to nitrogenase. Purification and characterization of pyruvate:flavodoxin oxidoreductase. The nifJ gene product. J. Biol. Chem. 258 (1983) 12064-12068. [PMID: 6352705]

2. Hughes, N.J., Clayton, C.L., Chalk, P.A. and Kelly, D.J. Helicobacter pylori porCDAB and oorDABC genes encode distinct pyruvate:flavodoxin and 2-oxoglutarate:acceptor oxidoreductases which mediate electron transport to NADP. J. Bacteriol. 180 (1998) 1119-1128. [PMID: 9495749]

3. Nakayama, T., Yonekura, S., Yonei, S. and Zhang-Akiyama, Q.M. Escherichia coli pyruvate:flavodoxin oxidoreductase, YdbK - regulation of expression and biological roles in protection against oxidative stress. Genes Genet. Syst. 88 (2013) 175-188. [PMID: 24025246]

4. Blaschkowski, H.P., Neuer, G., Ludwig-Festl, M. and Knappe, J. Routes of flavodoxin and ferredoxin reduction in Escherichia coli. CoA-acylating pyruvate: flavodoxin and NADPH: flavodoxin oxidoreductases participating in the activation of pyruvate formate-lyase. Eur. J. Biochem. 123 (1982) 563-569. [PMID: 7042345]

[EC 1.2.8.1 created 2025]


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