| UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.2.13 | ||||||||
| CAS no. | 2620865 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase ( EC 6.3.2.13, MurE synthetase, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-2,6-diamino-heptanedioate ligase (ADP-forming), UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelate synthetase, UDP-N-acetylmuramoylalanyl-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). [1] [2] This enzyme catalyses the following chemical reaction
- ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate
This enzyme takes part in synthesis of a cell-wall peptide.
References
- ^ Mizuno Y, Ito E (May 1968). "Purification and properties of uridine diphosphate N-acetylmuramyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate ligase". The Journal of Biological Chemistry. 243 (10): 2665–72. PMID 4967958.
- ^ van Heijenoort J (October 2001). "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Natural Product Reports. 18 (5): 503–19. doi: 10.1039/a804532a. PMID 11699883.
External links
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate+ligase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.2.13 | ||||||||
| CAS no. | 2620865 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase ( EC 6.3.2.13, MurE synthetase, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-2,6-diamino-heptanedioate ligase (ADP-forming), UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelate synthetase, UDP-N-acetylmuramoylalanyl-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). [1] [2] This enzyme catalyses the following chemical reaction
- ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate
This enzyme takes part in synthesis of a cell-wall peptide.
References
- ^ Mizuno Y, Ito E (May 1968). "Purification and properties of uridine diphosphate N-acetylmuramyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate ligase". The Journal of Biological Chemistry. 243 (10): 2665–72. PMID 4967958.
- ^ van Heijenoort J (October 2001). "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Natural Product Reports. 18 (5): 503–19. doi: 10.1039/a804532a. PMID 11699883.
External links
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate+ligase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)