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2-aminoethylphosphonate—pyruvate transaminase

2-aminoethylphosphonate—pyruvate transaminase

In enzymology, a 2-aminoethylphosphonate—pyruvate transaminase (EC 2.6.1.37 [25] ) is an enzyme that catalyzes the chemical reaction

(2-aminoethyl)phosphonate + pyruvate2-phosphonoacetaldehyde + L-alanine

Thus, the two substrates of this enzyme are (2-aminoethyl)phosphonate and pyruvate, whereas its two products are 2-phosphonoacetaldehyde and L-alanine.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is (2-aminoethyl)phosphonate:pyruvate aminotransferase. Other names in common use include (2-aminoethyl)phosphonate transaminase, (2-aminoethyl)phosphonate aminotransferase, (2-aminoethyl)phosphonic acid aminotransferase, 2-aminoethylphosphonate-pyruvate aminotransferase, 2-aminoethylphosphonate aminotransferase, 2-aminoethylphosphonate transaminase, AEP transaminase, and AEPT. This enzyme participates in aminophosphonate metabolism. It employs one cofactor, pyridoxal phosphate.

2-aminoethylphosphonate-pyruvate transaminase
Identifiers
EC number2.6.1.37 [9]
CAS number37277-91-1 [10]
Databases
IntEnzIntEnz view [11]
BRENDABRENDA entry [12]
ExPASyNiceZyme view [13]
KEGGKEGG entry [14]
MetaCycmetabolic pathway [15]
PRIAMprofile [16]
PDB structuresRCSB PDB [17] PDBe [18] PDBsum [19]
Gene OntologyAmiGO [20] / QuickGO [21]
Search
PMCarticles [22]
PubMedarticles [23]
NCBIproteins [24]

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1M32 [26] .

References

[1]
Citation Link//doi.org/10.1016%2F0304-4165%2868%2990223-710.1016/0304-4165(68)90223-7
Sep 25, 2019, 3:42 AM
[2]
Citation Link//www.ncbi.nlm.nih.gov/pubmed/49825004982500
Sep 25, 2019, 3:42 AM
[3]
Citation Link//doi.org/10.1111%2Fj.1432-1033.1983.tb07436.x10.1111/j.1432-1033.1983.tb07436.x
Sep 25, 2019, 3:42 AM
[4]
Citation Link//www.ncbi.nlm.nih.gov/pubmed/64062286406228
Sep 25, 2019, 3:42 AM
[5]
Citation Link//doi.org/10.1111%2Fj.1432-1033.1993.tb18100.x10.1111/j.1432-1033.1993.tb18100.x
Sep 25, 2019, 3:42 AM
[6]
Citation Link//www.ncbi.nlm.nih.gov/pubmed/83948138394813
Sep 25, 2019, 3:42 AM
[7]
Citation Link//doi.org/10.1099%2F00221287-138-6-128310.1099/00221287-138-6-1283
Sep 25, 2019, 3:42 AM
[8]
Citation Link//www.ncbi.nlm.nih.gov/pubmed/15274991527499
Sep 25, 2019, 3:42 AM
[9]
Citation Linkwww.qmul.ac.uk2.6.1.37
Sep 25, 2019, 3:42 AM
[10]
Citation Linkwww.commonchemistry.org37277-91-1
Sep 25, 2019, 3:42 AM
[11]
Citation Linkwww.ebi.ac.ukIntEnz view
Sep 25, 2019, 3:42 AM
[12]
Citation Linkwww.brenda-enzymes.orgBRENDA entry
Sep 25, 2019, 3:42 AM
[13]
Citation Linkwww.expasy.orgNiceZyme view
Sep 25, 2019, 3:42 AM
[14]
Citation Linkwww.genome.jpKEGG entry
Sep 25, 2019, 3:42 AM
[15]
Citation Linkbiocyc.orgmetabolic pathway
Sep 25, 2019, 3:42 AM
[16]
Citation Linkpriam.prabi.frprofile
Sep 25, 2019, 3:42 AM
[17]
Citation Linkwww.rcsb.orgRCSB PDB
Sep 25, 2019, 3:42 AM
[18]
Citation Linkwww.ebi.ac.ukPDBe
Sep 25, 2019, 3:42 AM
[19]
Citation Linkwww.ebi.ac.ukPDBsum
Sep 25, 2019, 3:42 AM
[20]
Citation Linkamigo.geneontology.orgAmiGO
Sep 25, 2019, 3:42 AM