Gene Review:
lysA - diaminopimelate decarboxylase
Escherichia coli CFT073
- Glycine betaine-assisted protein folding in a lysA mutant of Escherichia coli. Bourot, S., Sire, O., Trautwetter, A., Touzé, T., Wu, L.F., Blanco, C., Bernard, T. J. Biol. Chem. (2000)
- Nucleotide sequence and organization of the upstream region of the Corynebacterium glutamicum lysA gene. Marcel, T., Archer, J.A., Mengin-Lecreulx, D., Sinskey, A.J. Mol. Microbiol. (1990)
- Pseudomonas aeruginosa diaminopimelate decarboxylase: evolutionary relationship with other amino acid decarboxylases. Martin, C., Cami, B., Yeh, P., Stragier, P., Parsot, C., Patte, J.C. Mol. Biol. Evol. (1988)
- Cloning, expression and sequence analysis of an endolysin-encoding gene of Lactobacillus bulgaricus bacteriophage mv1. Boizet, B., Lahbib-Mansais, Y., Dupont, L., Ritzenthaler, P., Mata, M. Gene (1990)
- Cloning of the lysA gene from Mycobacterium tuberculosis. Andersen, A.B., Hansen, E.B. Gene (1993)
- Crystal structure of Mycobacterium tuberculosis diaminopimelate decarboxylase, an essential enzyme in bacterial lysine biosynthesis. Gokulan, K., Rupp, B., Pavelka, M.S., Jacobs, W.R., Sacchettini, J.C. J. Biol. Chem. (2003)
- Regulatory pattern of the Escherichia coli lysA gene: expression of chromosomal lysA-lacZ fusions. Stragier, P., Borne, F., Richaud, F., Richaud, C., Patte, J.C. J. Bacteriol. (1983)
- Heterologous expression and regulation of the lysA genes of Pseudomonas aeruginosa and Escherichia coli. Martin, C., Cami, B., Borne, F., Jeenes, D.J., Haas, D., Patte, J.C. Mol. Gen. Genet. (1986)
- Physiological and geometrical conditions for cell division in Escherichia coli. Woldringh, C.L., Valkendurg, J.A., Pas, E., Taschner, P.E., Huls, P., Wientjes, F.B. Ann. Inst. Pasteur Microbiol. (1985)
- Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli. I. Identification of a lysR gene encoding an activator of the lysA gene. Stragier, P., Richaud, F., Borne, F., Patte, J.C. J. Mol. Biol. (1983)
- Cloning and sequence analysis of the meso-diaminopimelate decarboxylase gene from Bacillus methanolicus MGA3 and comparison to other decarboxylase genes. Mills, D.A., Flickinger, M.C. Appl. Environ. Microbiol. (1993)
- Generation of an Escherichia coli lysA targeted deletion mutant by double cross-over recombination for potential use in a bacterial growth-based lysine assay. Li, X., Ricke, S.C. Lett. Appl. Microbiol. (2003)
- Molecular cloning and analysis of nucleotide sequence of the Bacillus subtilis lysA gene region using B. subtilis phage vectors and a multi-copy plasmid, pUB110. Yamamoto, J., Shimizu, M., Yamane, K. Agric. Biol. Chem. (1991)
- L-Lysine biosynthetic pathway of Methylophilus methylotrophus and construction of an L-lysine producer. Tsujimoto, N., Gunji, Y., Ogawa-Miyata, Y., Shimaoka, M., Yasueda, H. J. Biotechnol. (2006)
- The regulation of diaminopimelate decarboxylase activity in Escherichia coli strain w. White, P.J. J. Gen. Microbiol. (1976)
- Enzymic assays for isomers of 2,6-diaminopimelic acid in walls of Bacillus cereus and Bacillus megaterium. Day, A., White, P.J. Biochem. J. (1977)
- Crystallization of diaminopimelate decarboxylase from Escherichia coli, a stereospecific D-amino-acid decarboxylase. Momany, C., Levdikov, V., Blagova, L., Crews, K. Acta Crystallogr. D Biol. Crystallogr. (2002)