|Function||pyruvate formate-lyase 1-activating enzyme|
|Domain Trusted Cutoff||231.75|
|Domain Noise Cutoff||203.45|
|Mainrole Category||Energy metabolism|
|Gene Ontology Term||GO:0018307: enzyme active site formation biological_process|
| ||GO:0043365: [formate-C-acetyltransferase]-activating enzyme activity molecular_function|
|Entry Date||Feb 25 2005 3:34PM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||An iron-sulfur protein with a radical-SAM domain (PF04055). A single glycine residue in EC 184.108.40.206, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue .|
RM PMID: 8175649
RT Adenosylmethionine-dependent synthesis of the glycyl radical in pyruvate formate-lyase by abstraction of the glycine C-2 pro-S hydrogen atom. Studies of [2H]glycine-substituted enzyme and peptides homologous to the glycine 734 site.
RA Frey M, Rothe M, Wagner AF, Knappe J.
RL J Biol Chem. 1994 Apr 29;269(17):12432-7.|
|Genome Property||GenProp0943: pyruvate formate-lyase system (HMM)|
© J. Craig Venter Institute | Privacy Statement | Data Disclaimer