3-ketovalidoxylamine C-N-lyase

3-ketovalidoxylamine C-N-lyase
Identifiers
EC number	4.3.3.1
CAS number	99889-98-2
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

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.

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. PMID 4093450.