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-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
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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

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