EC 4.3.3.1 - 3-ketovalidoxylamine C-N-lyase

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IntEnz Enzyme Nomenclature
EC 4.3.3.1

Names

Accepted name:
3-ketovalidoxylamine C-N-lyase
Other names:
3-ketovalidoxylamine A C-N-lyase
p-nitrophenyl-3-ketovalidamine p-nitroaniline lyase
4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase
Systematic name:
4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase [5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one-forming]

Reaction

Cofactor

Comments:

Requires Ca2+. Eliminates 4-nitroaniline from 4-nitrophenyl-3-ketovalidamine, or 4-nitrophenol from 4-nitrophenyl-α-D-3-dehydroglucoside. Involved in the degradation of the fungicide validamycin A by Flavobacterium saccharophilum.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047566
CAS Registry Number: 99889-98-2

References

  1. Asano, N., Takeuchi, M., Ninomiya, K., Kameda, Y. and Matsui, K.
    Microbial degradation of validamycin A by Flavobacterium saccharophilum. Enzymatic cleavage of C-N linkage in validoxylamine A.
    J. Antibiot. 37 : 859-867 (1984). [PMID: 6548220]
  2. Takeuchi, M., Asano, N., Kameda, Y. and Matsui, K.
    Purification and properties of 3-ketovalidoxylamine A C-N lyase from Flavobacterium saccharophilum.
    J. Biochem. (Tokyo) 98 : 1631-1638 (1985). [PMID: 4093450]

[EC 4.3.3.1 created 1989]