The Enzyme Database

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EC 4.3.3.1     
Accepted name: 3-ketovalidoxylamine C-N-lyase
Reaction: 4-nitrophenyl-3-ketovalidamine = 4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one
Other name(s): 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]
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: BRENDA, EXPASY, KEGG, MetaCyc, 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 (1984) 859–867. [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 (1985) 1631–1638. [PMID: 4093450]
[EC 4.3.3.1 created 1989]
 
 


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