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Information on EC 1.1.3.44 - 6'''-hydroxyneomycin C oxidase and Organism(s) Streptomyces fradiae and UniProt Accession Q53U15

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IUBMB Comments
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.
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This record set is specific for:
Streptomyces fradiae
UNIPROT: Q53U15
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The taxonomic range for the selected organisms is: Streptomyces fradiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
neo-11, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
neoG
-
-
-
-
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.
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
about 15% of the rate with 6'''-deamino-6'''-hydroxyneomycin C
-
-
?
6'''-deamino-6'''-hydroxyneomycin C + O2
6'''-deamino-6'''-oxoneomycin C + H2O2
show the reaction diagram
additional information
?
-
enzyme also catalyzes reaction of EC 1.1.3.43, paromamine 6'-oxidase
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4
pH 7.5, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
joint activity of enzyme and 6'-oxoglucosaminyl:L-glutamate aminotransferase Neo-18 is responsible for the conversion of paromamine to neaminein the biosynthetic pathway of neomycin through a mechanism of FAD-dependent dehydrogenation followed by a pyridoxal-5'-phosphate-mediated transamination
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NEOG_STRFR
541
0
58004
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60034
x * 60034, LC-ESI-MS
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 60034, LC-ESI-MS
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Huang, F.; Spiteller, D.; Koorbanally, N.A.; Li, Y.; Llewellyn, N.M.; Spencer, J.B.
Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin
ChemBioChem
8
283-288
2007
Streptomyces fradiae (Q53U15), Streptomyces fradiae NCIMB 8233 (Q53U15)
Manually annotated by BRENDA team
Clausnitzer, D.; Piepersberg, W.; Wehmeier, U.F.
The oxidoreductases LivQ and NeoQ are responsible for the different 6-modifications in the aminoglycosides lividomycin and neomycin
J. Appl. Microbiol.
111
642-651
2011
Streptomyces fradiae (Q53U15), Streptomyces fradiae NCIMB 8233 (Q53U15), Streptomyces lividus (Q2MF66)
Manually annotated by BRENDA team