| EC |
2.6.1.83 |
| Accepted name: |
LL-diaminopimelate aminotransferase |
| Reaction: |
LL-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O |
|
For diagram of lysine biosynthesis (later stages), click here |
| Glossary: |
LL-diaminopimelate = LL-2,6-diaminoheptanedioate
tetrahydrodipicolinate = tetrahydropyridine-2,6-dicarboxylate |
| Other name(s): |
LL-diaminopimelate transaminase; LL-DAP aminotransferase; LL-DAP-AT |
| Systematic name: |
LL-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase |
| Comments: |
A pyridoxal-phosphate enzyme. In vivo, the reaction occurs in the opposite direction to that shown above. This is one of the final steps in the lysine-biosynthesis pathway of plants (ranging from mosses to flowering plants). meso-Diaminoheptanedioate, an isomer of LL-2,6-diaminoheptanedioate, and the structurally related compounds lysine and ornithine are not substrates. 2-Oxoglutarate cannot be replaced by oxaloacetate or pyruvate. It is not yet known if the substrate of the biosynthetic reaction is the cyclic or acyclic form of tetrahydropyridine-2,6-dicarboxylate. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 949001-34-7 |
| References: |
| 1. |
Hudson, A.O., Singh, B.K., Leustek, T. and Gilvarg, C. An LL-diaminopimelate aminotransferase defines a novel variant of the lysine biosynthesis pathway in plants. Plant Physiol. 140 (2006) 292–301. [DOI] [PMID: 16361515] |
|
| [EC 2.6.1.83 created 2006] |
| |
|
| |
|
| EC |
3.5.1.47 |
| Accepted name: |
N-acetyldiaminopimelate deacetylase |
| Reaction: |
N-acetyl-LL-2,6-diaminoheptanedioate + H2O = acetate + LL-2,6-diaminoheptanedioate |
| Other name(s): |
N-acetyl-L-diaminopimelic acid deacylase; N-acetyl-LL-diaminopimelate deacylase; 6-N-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase |
| Systematic name: |
N6-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 99193-93-8 |
| References: |
| 1. |
Bartlett, A.T.M. and White, P.J. Species of Bacillus that make a vegetative peptidoglycan containing lysine lack diaminopimelate epimerase but have diaminopimelate dehydrogenase. J. Gen. Microbiol. 131 (1985) 2145–2152. |
| 2. |
Saleh, F. and White, P.J. Metabolism of DD-2,6-diaminopimelic acid by a diaminopimelate-requiring mutant of Bacillus megaterium. J. Gen. Microbiol. 115 (1979) 95–100. |
| 3. |
Sundharadas, G. and Gilvarg, C. Biosynthesis of α,ε-diaminopimelic acid in Bacillus megaterium. J. Biol. Chem. 242 (1967) 3983–3984. [PMID: 4962540] |
|
| [EC 3.5.1.47 created 1984 (EC 3.1.1.62 created 1989, incorporated 1992)] |
| |
|
| |
|
Printable version