Formate acetyltransferase
| Formate acetyltransferase 1 ( E. coli ) | ||
|---|---|---|
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Existing structural data : 1cm5 , 1h16 , 1h17 , 1h18 , 1mzo , 1qhm , 2pfl , 3pfl |
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| Mass / length primary structure | 759 amino acids | |
| Secondary to quaternary structure | Homodimer | |
| Identifier | ||
| Gene name (s) | pfB (EcoGene) | |
| External IDs |
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| Enzyme classification | ||
| EC, category | 2.3.1.54 , transferase | |
| Response type | Transfer of an acetyl group | |
| Substrate | Pyruvate + CoA | |
| Products | Acetyl-CoA + formate | |
| Occurrence | ||
| Homology family | Formate acetyltransferase | |
| Parent taxon | bacteria | |
The enzyme formate acetyltransferase (formerly pyruvate formate lyase ) (PFL) catalyzes the reaction of pyruvate to acetyl-CoA and formate (anion of formic acid ). It is part of the anaerobic energy metabolism of some bacteria such as B. E. coli .
PFL has a glycyl radical in the active center . This is generated post-translationally by the PFL activase with the conversion of S-adenosylmethionine . It is easily destroyed by atmospheric oxygen.
See also
literature
- AF Wagner, M. Frey, FA Neugebauer, W. Schäfer, J. Knappe: The free radical in pyruvate formate-lyase is located on glycine-734. In: Proceedings of the National Academy of Sciences . Volume 89, Number 3, February 1992, pp. 996-1000, ISSN 0027-8424 . PMID 1310545 . PMC 48372 (free full text).