Enzyme

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     2. Transferases
        2.6 Transferring nitrogenous groups
            2.6.1 Transaminases
ID:2.6.1.77
Description:Taurine--pyruvate aminotransferase.
Prosite: PDOC00519;
PDB:
PDBScop

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.6.1.77
BRENDA Enzyme Link: BRENDA 2.6.1.77
KEGG Enzyme Link: KEGG2.6.1.77
BioCyc Enzyme Link: BioCyc 2.6.1.77
ExPASy Enzyme Link: ExPASy2.6.1.77
EC2PDB Enzyme Link: EC2PDB 2.6.1.77
ExplorEnz Enzyme Link: ExplorEnz 2.6.1.77
PRIAM enzyme-specific profiles Link: PRIAM 2.6.1.77
IntEnz Enzyme Link: IntEnz 2.6.1.77
MEDLINE Enzyme Link: MEDLINE 2.6.1.77
MSA:

2.6.1.77;

Phylogenetic Tree:

2.6.1.77;

Uniprot:
M-CSA:
RHEA:10420 pyruvate + taurine = L-alanine + sulfoacetaldehyde
RULE(radius=1) [*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[CH2;+0:6]-[NH2;+0:7]>>[*:1]-[CH;+0:2](-[*:3])-[NH2;+0:7].[*:5]-[CH;+0:6]=[O;H0;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Dissimilation of the C2 sulfonates.Cook AM, Denger K2002 Dec12471498
Genetic analysis of a Rhodobacter capsulatus gene region involved in utilization of taurine as a sulfur source.Masepohl B, Führer F, Klipp W2001 Nov 2711728723
Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila wadsworthia.Laue H, Cook AM2000 Dec11082195