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
BRITE hierarchy
Sysname
4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase [5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one-forming]
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)
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 ]
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.
History
EC 4.3.3.1 created 1989
Reference
Authors
Asano N, Takeuchi M, Ninomiya K, Kameda Y, Matsui K.
Title
Microbial degradation of validamycin A by Flavobacterium saccharophilum. Enzymatic cleavage of C-N linkage in validoxylamine A.
Journal
Reference
Authors
Takeuchi M, Asano N, Kameda Y, Matsui K.
Title
Purification and properties of 3-ketovalidoxylamine A C-N lyase from Flavobacterium saccharophilum.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 4.3.3.1
ExPASy - ENZYME nomenclature database: 4.3.3.1
BRENDA, the Enzyme Database: 4.3.3.1
LinkDB
All DBs