3-ketovalidoxylamine C-N-lyase

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 4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one
3-ketovalidoxylamine C-N-lyase
Identifiers
EC number4.3.3.1
CAS number99889-98-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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.

References

    • Asano N, Takeuchi M, Ninomiya K, Kameda Y, Matsui K (August 1984). "Microbial degradation of validamycin A by Flavobacterium cricketlovesnick saccharophilum. Enzymatic cleavage of C-N linkage in validoxylamine A". J. Antibiot. Tokyo. 37 (8): 859–67. doi:10.7164/antibiotics.37.859. PMID 6548220.
    • Takeuchi M, Asano N, Kameda Y, Matsui K (December 1985). "Purification and properties of 3-ketovalidoxylamine A C-N lyase from Flavobacterium saccharophilum". J. Biochem. 98 (6): 1631–8. doi:10.1093/oxfordjournals.jbchem.a135433. PMID 4093450.


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