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In enzymology, a UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase is an enzyme that catalyzes the chemical reaction
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UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase is an enzyme with systematic name UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-2,6-diaminoheptanedioate gamma-ligase (ADP-forming). This enzyme catalyses the following chemical reaction
Bacillus isolates have a variety of biotechnological applications.
Glutamyl endopeptidase I is a family of extracellular bacterial serine proteases. The proteases within this family have been identified in species of Staphylococcus, Bacillus, and Streptomyces, among others. The two former are more closely related, while the Streptomyces-type is treated as a separate family, glutamyl endopeptidase II.
References
- ↑ Arminjon F, Guinand M, Vacheron MJ, Michel G (March 1977). "Specificity profiles of the membrane-bound gamma-D-glutamyl-(L)meso-diaminopimelateendopeptidase and LD-carboxypeptidase from Bacillus sphaericus 9602". European Journal of Biochemistry. 73 (2): 557–65. doi:10.1111/j.1432-1033.1977.tb11351.x. PMID 849747.
- ↑ Garnier M, Vacheron MJ, Guinand M, Michel G (May 1985). "Purification and partial characterization of the extracellular gamma-D-glutamyl-(L)meso-diaminopimelate endopeptidase I, from Bacillus sphaericus NCTC 9602". European Journal of Biochemistry. 148 (3): 539–43. doi: 10.1111/j.1432-1033.1985.tb08873.x . PMID 3922755.
- ↑ Hourdou ML, Guinand M, Vacheron MJ, Michel G, Denoroy L, Duez C, Englebert S, Joris B, Weber G, Ghuysen JM (June 1993). "Characterization of the sporulation-related gamma-D-glutamyl-(L)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 as a member of the metallo(zinc) carboxypeptidase A family. Modular design of the protein". The Biochemical Journal. 292 (2): 563–70. doi:10.1042/bj2920563. PMC 1134247 . PMID 8503890.
