We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Synonyms
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Neo-11
-
neoQ
-
-
obsolete gene name
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6'''-deamino-6'''-hydroxyneomycin C + O2 = 6'''-deamino-6'''-oxoneomycin C + H2O2
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MetaCyc
neomycin biosynthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2'''-N-acetyl-6'''-hydroxyneomycin C + O2
2'''-N-acetyl-6'''-oxoneomycin C + H2O2
6'''-deamino-6'''-hydroxyneomycin C + O2
6'''-deamino-6'''-oxoneomycin C + H2O2
additional information
?
-
2'''-N-acetyl-6'''-hydroxyneomycin C + O2
2'''-N-acetyl-6'''-oxoneomycin C + H2O2
Substrates: about 15% of the rate with 6'''-deamino-6'''-hydroxyneomycin C
?
2'''-N-acetyl-6'''-hydroxyneomycin C + O2
2'''-N-acetyl-6'''-oxoneomycin C + H2O2
Substrates: about 15% of the rate with 6'''-deamino-6'''-hydroxyneomycin C
?
2'''-N-acetyl-6'''-hydroxyneomycin C + O2
2'''-N-acetyl-6'''-oxoneomycin C + H2O2
Substrates: less than 10% of the rate with 6'''-deamino-6'''-hydroxyneomycin C
?
6'''-deamino-6'''-hydroxyneomycin C + O2
6'''-deamino-6'''-oxoneomycin C + H2O2
Substrates: oxygen-dependent mechanism for the regeneration of the FAD cofactor
?
6'''-deamino-6'''-hydroxyneomycin C + O2
6'''-deamino-6'''-oxoneomycin C + H2O2
Substrates: -
?
6'''-deamino-6'''-hydroxyneomycin C + O2
6'''-deamino-6'''-oxoneomycin C + H2O2
Substrates: oxygen-dependent mechanism for the regeneration of the FAD cofactor
?
6'''-deamino-6'''-hydroxyneomycin C + O2
6'''-deamino-6'''-oxoneomycin C + H2O2
Substrates: -
?
6'''-deamino-6'''-hydroxyneomycin C + O2
6'''-deamino-6'''-oxoneomycin C + H2O2
Substrates: -
?
additional information
?
-
Substrates: enzyme also catalyzes reaction of EC 1.1.3.43, paromamine 6'-oxidase
?
additional information
?
-
Substrates: enzyme also catalyzes reaction of EC 1.1.3.43, paromamine 6'-oxidase
?
additional information
?
-
Substrates: enzyme does not catalyze the reaction of EC 1.1.3.43, paromamine 6'-oxidase
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3.5
pH 7.5, temperature not specified in the publication
6.4
pH 7.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LIVQ_STRLV
546
0
58907
Swiss-Prot
-
NEOG_STRFR
541
0
58004
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
60034
x * 60034, LC-ESI-MS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
x * 60034, LC-ESI-MS
?
-
x * 60034, LC-ESI-MS
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
brenda
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 lividus (Q2MF66), Streptomyces fradiae NCIMB 8233 (Q53U15)
brenda
html completed
show
top
