| Entry |
|
| Name |
3-ketovalidoxylamine C-N-lyase;
3-ketovalidoxylamine A C-N-lyase;
p-nitrophenyl-3-ketovalidamine p-nitroaniline lyase;
4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase |
| Class |
Lyases;
Carbon-nitrogen lyases;
Amine-lyases
 |
| Sysname |
4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase
[5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one-form
ing] |
| Reaction(IUBMB) |
4-nitrophenyl-3-ketovalidamine = 4-nitroaniline +
5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one
[RN:R04367] |
| Reaction(KEGG) |
R04367
 |
| Substrate |
4-nitrophenyl-3-ketovalidamine [CPD:C03995] |
| Product |
4-nitroaniline [CPD:C02126];
5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one
[CPD:C04815] |
| Cofactor |
Calcium [CPD:C00076] |
| Comment |
Requires Ca2+. Eliminates 4-nitroaniline from
4-nitrophenyl-3-ketovalidamine, or 4-nitrophenol from
4-nitrophenyl-alpha-D-3-dehydroglucoside. Involved in the
degradation of the fungicide validamycin A by Flavobacterium
saccharophilum. |
Reference Authors Title
Journal Organism
|
1 [PMID:6548220]
Asano N, Takeuchi M, Ninomiya K, Kameda Y, Matsui K.
Microbial degradation of validamycin A by Flavobacterium
saccharophilum. Enzymatic cleavage of C-N linkage in validoxylamine
A.
J. Antibiot. (Tokyo). 37 (1984) 859-67.
Flavobacterium saccharophilum |
Reference Authors Title
Journal Organism
|
2 [PMID:4093450]
Takeuchi M, Asano N, Kameda Y, Matsui K.
Purification and properties of 3-ketovalidoxylamine A C-N lyase from
Flavobacterium saccharophilum.
J. Biochem. (Tokyo). 98 (1985) 1631-8.
Flavobacterium saccharophilum |
| Other DBs |
ExplorEnz - The Enzyme Database: 4.3.3.1
IUBMB Enzyme Nomenclature: 4.3.3.1
ExPASy - ENZYME nomenclature database: 4.3.3.1
BRENDA, the Enzyme Database: 4.3.3.1
CAS: 99889-98-2 |