Enzyme

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     2. Transferases
        2.6 Transferring nitrogenous groups
            2.6.1 Transaminases
ID:2.6.1.37
Description:2-aminoethylphosphonate--pyruvate transaminase.
Alternative Name: 2-aminoethylphosphonate--pyruvate aminotransferase.
2-aminoethylphosphonate aminotransferase.
(2-aminoethyl)phosphonic acid aminotransferase.
(2-aminoethyl)phosphonate--pyruvate aminotransferase.
(2-aminoethyl)phosphonate transaminase.
Cath: 3.40.640.10; 3.90.1150.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.6.1.37
BRENDA Enzyme Link: BRENDA 2.6.1.37
KEGG Enzyme Link: KEGG2.6.1.37
BioCyc Enzyme Link: BioCyc 2.6.1.37
ExPASy Enzyme Link: ExPASy2.6.1.37
EC2PDB Enzyme Link: EC2PDB 2.6.1.37
ExplorEnz Enzyme Link: ExplorEnz 2.6.1.37
PRIAM enzyme-specific profiles Link: PRIAM 2.6.1.37
IntEnz Enzyme Link: IntEnz 2.6.1.37
MEDLINE Enzyme Link: MEDLINE 2.6.1.37
MSA:

2.6.1.37;

Phylogenetic Tree:

2.6.1.37;

Uniprot:
M-CSA:
RHEA:17021 (2-aminoethyl)phosphonate + pyruvate = L-alanine + phosphonoacetaldehyde
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
Stereochemistry of the reaction catalysed by 2-aminoethylphosphonate aminotransferase. A 1H-NMR study.Lacoste AM, Dumora C, Balas L, Hammerschmidt F, Vercauteren J1993 Aug 18394813
Purification and properties of 2-aminoethylphosphonate:pyruvate aminotransferase from Pseudomonas aeruginosa.Dumora C, Lacoste AM, Cassaigne A1983 Jun 16406228
The identification of 2-phosphonoacetaldehyde as an intermediate in the degradation of 2-aminoethylphosphonate by Bacillus cereus.La Nauze JM, Rosenberg H1968 Oct 154982500
Utilization of 2-aminoethylarsonic acid in Pseudomonas aeruginosa.Lacoste AM, Dumora C, Ali BR, Neuzil E, Dixon HB1992 Jun1527499