Enzyme

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     2. Transferases
        2.6 Transferring nitrogenous groups
            2.6.1 Transaminases
ID:2.6.1.112
Description:(S)-ureidoglycine--glyoxylate transaminase.
Alternative Name: UGXT.
(S)-ureidoglycine--glyoxylate aminotransferase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.6.1.112
BRENDA Enzyme Link: BRENDA 2.6.1.112
KEGG Enzyme Link: KEGG2.6.1.112
BioCyc Enzyme Link: BioCyc 2.6.1.112
ExPASy Enzyme Link: ExPASy2.6.1.112
EC2PDB Enzyme Link: EC2PDB 2.6.1.112
ExplorEnz Enzyme Link: ExplorEnz 2.6.1.112
PRIAM enzyme-specific profiles Link: PRIAM 2.6.1.112
IntEnz Enzyme Link: IntEnz 2.6.1.112
MEDLINE Enzyme Link: MEDLINE 2.6.1.112
MSA:

2.6.1.112;

Phylogenetic Tree:

2.6.1.112;

Uniprot:
M-CSA:
RHEA:33867 (S)-2-ureidoglycine + glyoxylate = glycine + N-carbamoyl-2-oxoglycine
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[*:5]-[CH;+0:6]=[O;H0;+0:7]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:7].[*:5]-[CH2;+0:6]-[NH2;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
An aminotransferase branch point connects purine catabolism to amino acid recycling.Ramazzina I, Costa R, Cendron L, Berni R, Peracchi A, Zanotti G, Percudani R2010 Nov20852637
Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator.Schultz AC, Nygaard P, Saxild HH2001 Jun11344136