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B6db activities:
Description LL-diaminopimelate aminotransferase
Alternative names LL-diaminopimelate transaminase;
Tetrahydrodipicolinate-glutamate aminotransferase.
Catalyzed reaction LL-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
Cofactor Pyridoxal-phosphate
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.
An enzyme involved in L-Lysine biosynthesis in plants and Chlamidia. It specifically catalyzes the interconversion of tetrahydrodipicolinate and LL-diaminopimelate, a process requiring three separate enzymes (including succinyldiaminopimelate aminotransferase - EC in the Lysine biosynthetic pathway found in Escherichia coli.
PDB 2Z1Z; 2Z20;
Organisms -Eubacteria -Archea -Plants


Links Enzyme (activities)
BRENDA (activities)
KEGG (pathways)
PLPMDB (PLP mutants)
 Liu Y, White RH, Whitman WB. (2010) Methanococci use the diaminopimelate aminotransferase (DapL) pathway for lysine biosynthesis J Bacteriol 192 3304-10.

 Graham DE, Huse HK. (2008) Methanogens with pseudomurein use diaminopimelate aminotransferase in lysine biosynthesis FEBS Lett 3582 1369-74.

 Hudson AO, Gilvarg C, Leustek T. (2008) Biochemical and phylogenetic characterization of a novel diaminopimelate biosynthesis pathway in prokaryotes identifies a diverged form of LL-diaminopimelate aminotransferase J Bacteriol 190 3256-63.

 Watanabe N, Cherney MM, van Belkum MJ, Marcus SL, Flegel MD, Clay MD, Deyholos MK, Vederas JC, James MN. (2007) Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia J Mol Biol 371 685-702.

 Hudson AO, Singh BK, Leustek T, Gilvarg C. (2006) An LL-diaminopimelate aminotransferase defines a novel variant of the lysine biosynthesis pathway in plants Plant Physiol 140 292-301.

 McCoy AJ, Adams NE, Hudson AO, Gilvarg C, Leustek T, Maurelli AT. (2006) L,L-diaminopimelate aminotransferase, a trans-kingdom enzyme shared by Chlamydia and plants for synthesis of diaminopimelate/lysine Proc Natl Acad Sci U S A 103 17909-14.

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last changed 2010/02/02 10:28

B6db activities