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B6db activities:
Description Diaminopimelate decarboxylase
Alternative names meso-diaminopimelate decarboxylase;
meso-diaminopimelic acid decarboxylase;
DAP decarboxylase;
Catalyzed reaction Meso-2,6-diaminoheptanedioate = L-lysine + CO(2).
Cofactor Pyridoxal-phosphate.
Comments Bacteria have developed at least three different routes to synthesize lysine from aspartate, but in each of these routes lysine is ultimately produced by decarboxylating diaminopimelate (DAP), a metabolite that is also involved in peptidoglycan formation.

DAP is a symmetric molecule, containing two alpha carbons - one in configuration L, the other in configuration D. The enzyme selectively removes the carboxylate group from the latter, to generate L-lysine.
Thus, diaminopimelate decarboxylase is a rare case of PLP-dependent D-amino-acid decarboxylase, together with the strictly related D-ornithine/D-lysine decarboxylase (

Prosite PROSITE; PDOC00685;
Organisms -Eubacteria -Archea -Plants

Family (0)
Links Enzyme (activities)
BRENDA (activities)
KEGG (pathways)
PLPMDB (PLP mutants)
 Son HF, Kim KJ (2018) Structural basis for substrate specificity of meso-diaminopimelic acid decarboxylase from Corynebacterium glutamicum Biochem Biophys Res Commun 495 1815-1821.

 Peverelli MG, Soares da Costa TP, Kirby N, Perugini MA (2016) Dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis J Biol Chem 291 9785-95.

 Oliver MR, Crowther JM, Leeman MM, Kessans SA, North RA, Donovan KA, Griffin MD, Suzuki H, Hudson AO, Kasanmascheff M, Dobson RC (2014) The purification, crystallization and preliminary X-ray diffraction analysis of two isoforms of meso-diaminopimelate decarboxylase from Arabidopsis thaliana Acta Crystallogr F Struct Biol Commun. 70 663-8.

 Tsujimoto N, Gunji Y, Ogawa-Miyata Y, Shimaoka M, Yasueda H. (2006) L-Lysine biosynthetic pathway of Methylophilus methylotrophus and construction of an L-lysine producer J Biotechnol 124 327-37.

 Hudson AO, Bless C, Macedo P, Chatterjee SP, Singh BK, Gilvarg C, Leustek T. (2005) Biosynthesis of lysine in plants: evidence for a variant of the known bacterial pathways Biochim Biophys Acta 1721 27-36.

 Gokulan, K.; Rupp, B.; Pavelka, M.S. Jr,; Jacobs, W.R. Jr; Sacchettini, J.C. (2003) Crystal structure of Mycobacterium tuberculosis diaminopimelate decarboxylase, an essential enzyme in bacterial lysine biosynthesis J Biol Chem 278 18588-96.

 Ray, S.S.; Bonanno JB, Rajashankar KR, Pinho MG, He G, De Lencastre H, Tomasz A, Burley S.K. (2002) Cocrystal structures of diaminopimelate decarboxylase: mechanism, evolution, and inhibition of an antibiotic resistance accessory factor Structure (Camb) 10 1499-508.

 Scapin, G.; Blanchard, J.S. (1998) Enzymology of bacterial lysine biosynthesis Adv Enzymol Relat Areas Mol Biol 72 279-324.

 Mills, D. A.; Flickinger, M. C. (1993) Cloning and sequence analysis of the meso-diaminopimelate decarboxylase gene from Bacillus methanolicus MGA3 and comparison to other decarboxylase genes Appl Environ Microbiol 59 2927-37.

 Martin, C.; Cami, B.; Borne, F.; Jeenes, D.J.; Haas, D.; Patte, J.C. (1986) Heterologous expression and regulation of the lysA genes of Pseudomonas aeruginosa and Escherichia coli Mol Gen Genet 203 430-4.

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last changed 2019/05/29 09:37

B6db activities