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B6db activities: 2.6.1.83

2.6.1.83
Description LL-diaminopimelate aminotransferase
Alternative names LL-diaminopimelate transaminase;
LL-DAP-aminotransferase;
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 2.6.1.17) in the Lysine biosynthetic pathway found in Escherichia coli.
PDB 2Z1Z; 2Z20;
Organisms -Eubacteria -Archea -Plants
 

Family 

 
Links Enzyme (activities) 2.6.1.83
BRENDA (activities) 2.6.1.83
KEGG (pathways) 2.6.1.83
PLPMDB (PLP mutants) 2.6.1.83
 
References
 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.

Articles on 2.6.1.83
 
last changed 2010/02/02 10:28

B6db activities