| (Carboxyethyl)arginine β-lactam-synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 beta-lactam synthetase. PDB 1mc1
[1] | |||||||||
| Identifiers | |||||||||
| EC no. | 6.3.3.4 | ||||||||
| CAS no. | 68247-54-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a (carboxyethyl)arginine β-lactam-synthase ( EC 6.3.3.4) is an enzyme that catalyzes the chemical reaction
arginine_beta-lactam-synthase.svg)
- ATP + L-N2-(2-carboxyethyl)arginine AMP + diphosphate + deoxyamidinoproclavaminate
Thus, the two substrates of this enzyme are ATP and L-N2-(2-carboxyethyl)arginine, whereas its 3 products are AMP, diphosphate, and deoxyamidinoproclavaminate.
This enzyme belongs to the family of ligases, specifically the cyclo-ligases, which form carbon-nitrogen bonds. The systematic name of this enzyme class is L-N2-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming). This enzyme is also called L-2-N-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming). This enzyme participates in clavulanic acid biosynthesis.
- ^ Miller, M. T.; Bachmann, B. O.; Townsend, C. A.; Rosenzweig, A. C. (2002). "The catalytic cycle of beta -lactam synthetase observed by x-ray crystallographic snapshots". Proceedings of the National Academy of Sciences. 99 (23): 14752–14757. Bibcode: 2002PNAS...9914752M. doi: 10.1073/pnas.232361199. PMC 137491. PMID 12409610.
- Zhou J, Kelly WL, Bachmann BO, Gunsior M, Townsend CA, Solomon EI (2001). "Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional alpha-KG-dependent non-heme iron enzyme: correlation with mechanisms and reactivities". J. Am. Chem. Soc. 123 (30): 7388–98. doi: 10.1021/ja004025+. PMID 11472170.
- Townsend CA (2002). "New reactions in clavulanic acid biosynthesis". Curr. Opin. Chem. Biol. 6 (5): 583–9. doi: 10.1016/S1367-5931(02)00392-7. PMID 12413541.
- Bachmann BO, Li R, Townsend CA (1998). "β-Lactam synthetase: A new biosynthetic enzyme". Proc. Natl. Acad. Sci. 95 (16): 9082–6. Bibcode: 1998PNAS...95.9082B. doi: 10.1073/pnas.95.16.9082. PMC 21295. PMID 9689037.
| (Carboxyethyl)arginine β-lactam-synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
|
beta-lactam synthetase. PDB 1mc1
[1] | |||||||||
| Identifiers | |||||||||
| EC no. | 6.3.3.4 | ||||||||
| CAS no. | 68247-54-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a (carboxyethyl)arginine β-lactam-synthase ( EC 6.3.3.4) is an enzyme that catalyzes the chemical reaction
- ATP + L-N2-(2-carboxyethyl)arginine AMP + diphosphate + deoxyamidinoproclavaminate
Thus, the two substrates of this enzyme are ATP and L-N2-(2-carboxyethyl)arginine, whereas its 3 products are AMP, diphosphate, and deoxyamidinoproclavaminate.
This enzyme belongs to the family of ligases, specifically the cyclo-ligases, which form carbon-nitrogen bonds. The systematic name of this enzyme class is L-N2-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming). This enzyme is also called L-2-N-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming). This enzyme participates in clavulanic acid biosynthesis.
- ^ Miller, M. T.; Bachmann, B. O.; Townsend, C. A.; Rosenzweig, A. C. (2002). "The catalytic cycle of beta -lactam synthetase observed by x-ray crystallographic snapshots". Proceedings of the National Academy of Sciences. 99 (23): 14752–14757. Bibcode: 2002PNAS...9914752M. doi: 10.1073/pnas.232361199. PMC 137491. PMID 12409610.
- Zhou J, Kelly WL, Bachmann BO, Gunsior M, Townsend CA, Solomon EI (2001). "Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional alpha-KG-dependent non-heme iron enzyme: correlation with mechanisms and reactivities". J. Am. Chem. Soc. 123 (30): 7388–98. doi: 10.1021/ja004025+. PMID 11472170.
- Townsend CA (2002). "New reactions in clavulanic acid biosynthesis". Curr. Opin. Chem. Biol. 6 (5): 583–9. doi: 10.1016/S1367-5931(02)00392-7. PMID 12413541.
- Bachmann BO, Li R, Townsend CA (1998). "β-Lactam synthetase: A new biosynthetic enzyme". Proc. Natl. Acad. Sci. 95 (16): 9082–6. Bibcode: 1998PNAS...95.9082B. doi: 10.1073/pnas.95.16.9082. PMC 21295. PMID 9689037.