Information on EC 1.1.3.44 - 6'''-hydroxyneomycin C oxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.3.44
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RECOMMENDED NAME
GeneOntology No.
6'''-hydroxyneomycin C oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
6'''-deamino-6'''-hydroxyneomycin C + O2 = 6'''-deamino-6'''-oxoneomycin C + H2O2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
neomycin biosynthesis
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Neomycin, kanamycin and gentamicin biosynthesis
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
6'''-deamino-6'''-hydroxyneomycin C:oxygen 6'''-oxidoreductase
Contains FAD. Involved in the biosynthetic pathway of aminoglycoside antibiotics of the neomycin family. Works in combination with EC 2.6.1.95, neomycin C transaminase, to replace the 6'''-hydroxy group of 6'''-hydroxyneomycin C with an amino group. Also catalyses EC 1.1.3.43, paromamine 6'-oxidase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'''-N-acetyl-6'''-hydroxyneomycin C + O2
2'''-N-acetyl-6'''-oxoneomycin C + H2O2
show the reaction diagram
6'''-deamino-6'''-hydroxyneomycin C + O2
6'''-deamino-6'''-oxoneomycin C + H2O2
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
pH 7.5, temperature not specified in the publication
6.4
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pH 7.5, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60034
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x * 60034, LC-ESI-MS
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
development of a coupled enzyme assays including 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazoliumbromide and phenazine methosulfate, resulting in the production of 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazoliumbromide formazan which can be monitored at 570 nm