EC number:1.21.4.2

Enzyme

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     1. Oxidoreductases
        1.21 Catalysing the reaction X-H + Y-H = X-Y
            1.21.4 With a disulfide as acceptor
ID:1.21.4.2
Description:Glycine reductase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.21.4.2
BRENDA Enzyme Link: BRENDA 1.21.4.2
KEGG Enzyme Link: KEGG1.21.4.2
BioCyc Enzyme Link: BioCyc 1.21.4.2
ExPASy Enzyme Link: ExPASy1.21.4.2
EC2PDB Enzyme Link: EC2PDB 1.21.4.2
ExplorEnz Enzyme Link: ExplorEnz 1.21.4.2
PRIAM enzyme-specific profiles Link: PRIAM 1.21.4.2
IntEnz Enzyme Link: IntEnz 1.21.4.2
MEDLINE Enzyme Link: MEDLINE 1.21.4.2

EC number:1.21.4.2

MSA:

1.21.4.2;
Phylogenetic Tree:

1.21.4.2;
Uniprot:
M-CSA:
RHEA:12232 [thioredoxin]-disulfide + acetyl phosphate + H2O + NH4(+) = [thioredoxin]-dithiol + glycine + H(+) + phosphate
RULE(radius=1) [*:1]-[S;H0;+0:2]-[S;H0;+0:3]-[*:4].[*:5]=[C;H0;+0:6](-[CH3;+0:7])-[O;H0;+0:8]-[*:9].[NH3;+0:10].[OH2;+0:11]>>[*:9]-[OH;+0:8].[*:4]-[SH;+0:3].[*:1]-[SH;+0:2].[*:5]=[C;H0;+0:6](-[OH;+0:11])-[CH2;+0:7]-[NH2;+0:10]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis.Wagner M, Sonntag D, Grimm R, Pich A, Eckerskorn C, Söhling B, Andreesen JR1999 Feb10091582