The Enzyme Database

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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. [PMID: 16361515]
[EC 2.6.1.83 created 2006]
 
 


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