KEGG   ENZYME: 4.3.3.1Help
Entry
EC 4.3.3.1                  Enzyme                                 

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
1  [PMID:6548220]
  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
J. Antibiot. (Tokyo). 37 (1984) 859-67.
Reference
2  [PMID:4093450]
  Authors
Takeuchi M, Asano N, Kameda Y, Matsui K.
  Title
Purification and properties of 3-ketovalidoxylamine A C-N lyase from Flavobacterium saccharophilum.
  Journal
J. Biochem. (Tokyo). 98 (1985) 1631-8.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
99889-98-2

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