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2.6.1.17 |
Description |
Succinyldiaminopimelate aminotransferase |
Alternative names |
Succinyldiaminopimelate transaminase;
N-succinyl-L,L-diaminopimelate aminotransferase;
N-succinyl-L,L-DAP aminotransferase;
DapC (gene name);
TabD (gene name);
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Catalyzed reaction |
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl- L-2-amino-6-oxoheptanedioate + L-glutamate. |
Cofactor |
Pyridoxal-phosphate. |
Comments |
In E. coli, this activity is carried out also by the enzyme that catalyzes the acetylornitine transaminase reaction (2.6.1.11) |
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The gene coding for succinyldiaminopimelate aminotransferase in bacteria is termed DapC. However in the literature confusion still exists regarding the gene acronym-enzyme relationships of the dapC and dapD genes, and in several database annotations dapD genes are still incorrectly reported to encode the N-succinyl-L,L-diaminopimelate aminotransferase.
An enzyme from M. tuberculosis, whose structure has been solved (PDB 2O0R) and which is assumed to possess N-succinyl-L,L-diaminopimelate aminotransferase activity, does not show a high similarity to the only functionally-validated DapC gene (from Bordetella) but rather to enzymes with kynurenine aminotransferase activity (EC 2.6.1.7). |
Prosite |
PROSITE; PDOC00094; |
PDB |
2O0R; |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) 2.6.1.17
BRENDA (activities) 2.6.1.17
KEGG (pathways) 2.6.1.17
PLPMDB (PLP mutants) 2.6.1.17
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References |
Manning ME, Danson EJ, Calderone CT (2018) Functional chararacterization of the enzymes TabB and TabD involved in tabtoxin biosynthesis by Pseudomonas syringae Biochem Biophys Res Commun 496 212-217. Weyand S, Kefala G, Weiss MS. (2007) The three-dimensional structure of N-succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis. J Mol Biol. 367 825-38. Marienhagen J, Kennerknecht N, Sahm H, Eggeling L. (2005) Functional analysis of all aminotransferase proteins inferred from the genome sequence of Corynebacterium glutamicum J Bacteriol 187 7639-46. Hartmann M, Tauch A, Eggeling L, Bathe B, Mockel B, Puhler A, Kalinowski J. (2003) Identification and characterization of the last two unknown genes, dapC and dapF, in the succinylase branch of the L-lysine biosynthesis of Corynebacterium glutamicum J Biotechnol 104 199-211. Cox, R.J.
Wang, P.S.H. (2001) Is N-acetylornithine aminotransferase the real N-succinyl-LL-diaminopimelate aminotransferase in Escherichia coli and Mycobacterium smegmatis? J. Chem Soc-Perkin Transactions 1 2001 2006-2008. Fuchs, T. M.; Schneider, B.; Krumbach, K.; Eggeling, L.; Gross, R. (2000) Characterization of a bordetella pertussis diaminopimelate (DAP) biosynthesis locus identifies dapC, a novel gene coding for an N- succinyl-L,L-DAP aminotransferase J Bacteriol 182 3626-31. Articles on 2.6.1.17 |
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last changed |
2018/12/20 10:56 |
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