3-ketovalidoxylamine C-N-lyase

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In enzymology, a 3-ketovalidoxylamine C-N-lyase (EC 4.3.3.1) is an enzyme that catalyzes the chemical reaction

4-nitrophenyl-3-ketovalidamine $\rightleftharpoons$ 4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one

Hence, this enzyme has one substrate, 4-nitrophenyl-3-ketovalidamine, and two products, 4-nitroaniline and 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one.

This enzyme belongs to the family of lyases, specifically amine lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is 4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase [5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one-form ing]. Other names in common use include 3-ketovalidoxylamine A C-N-lyase, p-nitrophenyl-3-ketovalidamine p-nitroaniline lyase, and 4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase. It employs one cofactor, calcium.

[edit] References

IUBMB entry for 4.3.3.1
BRENDA references for 4.3.3.1 (Recommended.)
PubMed references for 4.3.3.1
PubMed Central references for 4.3.3.1
Google Scholar references for 4.3.3.1
Asano N, Takeuchi M, Ninomiya K, Kameda Y, Matsui K (Tokyo). "Microbial degradation of validamycin A by Flavobacterium cricketlovesnick saccharophilum. Enzymatic cleavage of C-N linkage in validoxylamine A". J. Antibiot.: 859–67. PMID 6548220.
Takeuchi M, Asano N, Kameda Y, Matsui K (Tokyo). "Purification and properties of 3-ketovalidoxylamine A C-N lyase from Flavobacterium saccharophilum". J. Biochem.: 1631–8. PMID 4093450.