Biology:L,L-diaminopimelate aminotransferase
| L,L-diaminopimelate aminotransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.6.1.83 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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L,L-diaminopimelate aminotransferase (EC 2.6.1.83) is a pyridoxal phosphate-dependent enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
The three substrates of this enzyme characterised from plants are (S)-2,3,4,5-tetrahydrodipicolinic acid (1), L-glutamic acid, and water. Its products are (S,S)-2,6-diaminopimelic acid a.k.a. L,L-diaminopimelic acid (2) and α-ketoglutaric acid. The product (2) goes on in a biosynthetic pathway leading to the amino acid lysine.[1]
This enzyme is a transferases, specifically a transaminase, which transfer nitrogenous groups. The systematic name of this enzyme class is LL-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase. Other names in common use include LL-diaminopimelate transaminase, LL-DAP aminotransferase, and LL-DAP-AT.[2]
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2Z1Z and 2Z20.
References
- ↑ "An LL-diaminopimelate aminotransferase defines a novel variant of the lysine biosynthesis pathway in plants". Plant Physiol. 140 (1): 292–301. 2006. doi:10.1104/pp.105.072629. PMID 16361515.
- ↑ Enzyme 2.6.1.83 at KEGG Pathway Database.
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