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==References==
==References==
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* {{cite journal | author = Knappe J, Blaschkowski HP, Grobner P, Schmitt T | date = 1974 | title = Pyruvate formate-lyase of Escherichia coli: the acetyl-enzyme intermediate | journal = Eur. J. Biochem. | volume = 50 | pages = 253–63 | pmid = 4615902 | doi = 10.1111/j.1432-1033.1974.tb03894.x }}
* {{cite journal | author = Knappe J, Blaschkowski HP, Grobner P, Schmitt T | date = 1974 | title = Pyruvate formate-lyase of Escherichia coli: the acetyl-enzyme intermediate | journal = Eur. J. Biochem. | volume = 50 | pages = 253–63 | pmid = 4615902 | doi = 10.1111/j.1432-1033.1974.tb03894.x | issue = 1 }}


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Revision as of 08:17, 28 June 2010

formate C-acetyltransferase
Identifiers
EC no.2.3.1.54
CAS no.9068-08-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a formate C-acetyltransferase (EC 2.3.1.54) is an enzyme that catalyzes the chemical reaction

acetyl-CoA + formate CoA + pyruvate

Thus, the two substrates of this enzyme are acetyl-CoA and formate, whereas its two products are CoA and pyruvate.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:formate C-acetyltransferase. Other names in common use include pyruvate formate-lyase, pyruvic formate-lyase, and formate acetyltransferase. This enzyme participates in 3 metabolic pathways: pyruvate metabolism, propanoate metabolism, and butanoate metabolism.

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1CM5, 1H16, 1H17, 1H18, 1MZO, 1QHM, 2PFL, and 3PFL.

References

  • Knappe J, Blaschkowski HP, Grobner P, Schmitt T (1974). "Pyruvate formate-lyase of Escherichia coli: the acetyl-enzyme intermediate". Eur. J. Biochem. 50 (1): 253–63. doi:10.1111/j.1432-1033.1974.tb03894.x. PMID 4615902.{{cite journal}}: CS1 maint: multiple names: authors list (link)