KEGG   ENZYME: 4.3.3.1
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
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)
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]
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) 37:859-67 (1984)
DOI:10.7164/antibiotics.37.859
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) 98:1631-8 (1985)
DOI:10.1093/oxfordjournals.jbchem.a135433
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

  All links  
Chemical substance (3)   
   KEGG COMPOUND (3)   
Chemical reaction (3)   
   KEGG REACTION (1)   
   KEGG RCLASS (2)   
All databases (6)   

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