3-ketovalidoxylamine C-N-lyase
| 3-ketovalidoxylamine C-N-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.3.3.1 | ||||||||
| CAS no. | 99889-98-2 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme 3-ketovalidoxylamine C-N-lyase (EC 4.3.3.1) catalyzes the chemical reaction
- 4-nitrophenyl-3-ketovalidamine 4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one
This enzyme belongs to the family of lyases, specifically amine lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is 4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase [5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one-forming]. Other names in common use include 3-ketovalidoxylamine A C-N-lyase, p-nitrophenyl-3-ketovalidamine p-nitroaniline lyase, and 4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase. It employs one cofactor, Ca2+.
References[edit]
- Asano N, Takeuchi M, Ninomiya K, Kameda Y, Matsui K (August 1984). "Microbial degradation of validamycin A by Flavobacterium saccharophilum. Enzymatic cleavage of C-N linkage in validoxylamine A". J. Antibiot. 37 (8). Tokyo: 859–67. doi:10.7164/antibiotics.37.859. PMID 6548220.
- Takeuchi M, Asano N, Kameda Y, Matsui K (December 1985). "Purification and properties of 3-ketovalidoxylamine A C-N lyase from Flavobacterium saccharophilum". J. Biochem. 98 (6): 1631–8. doi:10.1093/oxfordjournals.jbchem.a135433. PMID 4093450.
