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B6db activities: 4.1.1.20

4.1.1.20
Description Diaminopimelate decarboxylase.
Alternative names 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 the only known PLP-dependent D-amino-acid decarboxylase. However, several other fold-type III enzymes are known to act on D-amino acid substrates (e.g., alanine racemase or D-threonine aldolase).

Prosite PROSITE; PDOC00685;
PDB 1HKW; 1TWI;
Organisms -Bacteria -Archea -Plants
 

Family 

4.1.1.20 (43)
 
Links Enzyme (activities) 4.1.1.20
BRENDA (activities) 4.1.1.20
KEGG (pathways) 4.1.1.20
PLPMDB (PLP mutants) 4.1.1.20
 
References
 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.

Articles on 4.1.1.20
 
last changed 2009/06/08 14:27

B6db activities