Enzyme

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     1. Oxidoreductases
        1.97 Other oxidoreductases
            1.97.1 Sole sub-subclass for oxidoreductases that do not belong in the other subclasses
ID:1.97.1.4
Description:[Formate-C-acetyltransferase]-activating enzyme.
Alternative Name: Pyruvate formate-lyase 1 activating enzyme.
S-adenosyl-L-methionine-cleaving).
PFL-glycine:S-adenosyl-L-methionine H transferase (flavodoxin-oxidizing,
PFL activase.
methionine oxidoreductase (S-adenosyl-L-methionine cleaving).
Formate acetyltransferase-glycine dihydroflavodoxin:S-adenosyl-L-
Formate acetyltransferase activating enzyme.
[Pyruvate formate-lyase]-activating enzyme.
Prosite: PDOC00834;
PDB:
PDBScop
3CB8
3C8F
Cath: 3.20.20.70;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.97.1.4
BRENDA Enzyme Link: BRENDA 1.97.1.4
KEGG Enzyme Link: KEGG1.97.1.4
BioCyc Enzyme Link: BioCyc 1.97.1.4
ExPASy Enzyme Link: ExPASy1.97.1.4
EC2PDB Enzyme Link: EC2PDB 1.97.1.4
ExplorEnz Enzyme Link: ExplorEnz 1.97.1.4
PRIAM enzyme-specific profiles Link: PRIAM 1.97.1.4
IntEnz Enzyme Link: IntEnz 1.97.1.4
MEDLINE Enzyme Link: MEDLINE 1.97.1.4
MSA:

1.97.1.4;

Phylogenetic Tree:

1.97.1.4;

Uniprot:
M-CSA:
RHEA:19225 [formate C-acetyltransferase]-glycine + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + [formate C-acetyltransferase]-glycin-2-yl radical + H(+) + L-methionine + semiquinone [flavodoxin]
RULE(radius=1) [*:1]-[S+;H0:2](-[*:3])-[CH2;+0:4]-[*:5]>>[*:5]-[CH3;+0:4].[*:1]-[S;H0;+0:2]-[*:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
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.Frey M, Rothe M, Wagner AF, Knappe J1994 Apr 298175649
Structural basis for glycyl radical formation by pyruvate formate-lyase activating enzyme.Vey JL, Yang J, Li M, Broderick WE, Broderick JB, Drennan CL2008 Oct 2118852451
The free radical in pyruvate formate-lyase is located on glycine-734.Wagner AF, Frey M, Neugebauer FA, Schäfer W, Knappe J1992 Feb 11310545
Radical mechanisms of enzymatic catalysis.Frey PA200111395404