| EC Tree |
| 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: |
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| Cath: | 3.20.20.70; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| 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 |
| 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 |
| Title | Authors | Date | PubMed 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 J | 1994 Apr 29 | 8175649 |
| Structural basis for glycyl radical formation by pyruvate formate-lyase activating enzyme. | Vey JL, Yang J, Li M, Broderick WE, Broderick JB, Drennan CL | 2008 Oct 21 | 18852451 |
| The free radical in pyruvate formate-lyase is located on glycine-734. | Wagner AF, Frey M, Neugebauer FA, Schäfer W, Knappe J | 1992 Feb 1 | 1310545 |
| Radical mechanisms of enzymatic catalysis. | Frey PA | 2001 | 11395404 |