- Source: 2-oxobutyrate synthase
In enzymology, a 2-oxobutyrate synthase (EC 1.2.7.2) is an enzyme that catalyzes the chemical reaction
2-oxobutanoate + CoA + oxidized ferredoxin
⇌
{\displaystyle \rightleftharpoons }
propanoyl-CoA + CO2 + reduced ferredoxin
The 3 substrates of this enzyme are 2-oxobutanoate, CoA, and oxidized ferredoxin, whereas its 3 products are propanoyl-CoA, CO2, and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is 2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propanoylating). Other names in common use include alpha-ketobutyrate-ferredoxin oxidoreductase, 2-ketobutyrate synthase, alpha-ketobutyrate synthase, 2-oxobutyrate-ferredoxin oxidoreductase, and 2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propionylating). This enzyme participates in propanoate metabolism.
References
Buchanan BB (August 1969). "Role of ferredoxin in the synthesis of alpha-ketobutyrate from propionyl coenzyme A and carbon dioxide by enzymes from photosynthetic and nonphotosynthetic bacteria". The Journal of Biological Chemistry. 244 (15): 4218–23. PMID 5800441.