BRENDA - Enzyme Database

The oxidoreductases LivQ and NeoQ are responsible for the different 6-modifications in the aminoglycosides lividomycin and neomycin

Clausnitzer, D.; Piepersberg, W.; Wehmeier, U.F.; J. Appl. Microbiol. 111, 642-651 (2011)

Data extracted from this reference:

Application
EC Number
Application
Commentary
Organism
1.1.3.43
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
Streptomyces fradiae
1.1.3.44
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
Streptomyces lividus
Cloned(Commentary)
EC Number
Cloned (Commentary)
Organism
1.1.3.43
expression in Escherichia coli
Streptomyces fradiae
1.1.3.44
expression in Escherichia coli
Streptomyces fradiae
1.1.3.44
expression in Escherichia coli
Streptomyces lividus
2.6.1.93
expressed in Escherichia coli
Streptomyces fradiae
2.6.1.95
expressed in Escherichia coli
Streptomyces fradiae
Organism
EC Number
Organism
UniProt
Commentary
Textmining
1.1.3.43
Streptomyces fradiae
Q53U15
-
-
1.1.3.43
Streptomyces fradiae NCIMB 8233
Q53U15
-
-
1.1.3.44
Streptomyces fradiae
Q53U15
-
-
1.1.3.44
Streptomyces fradiae NCIMB 8233
Q53U15
-
-
1.1.3.44
Streptomyces lividus
Q2MF66
-
-
2.6.1.93
Streptomyces fradiae
-
-
-
2.6.1.95
Streptomyces fradiae
-
-
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.1.3.43
4.2
-
pH 7.5, temperature not specified in the publication
Streptomyces fradiae
1.1.3.44
3.5
-
pH 7.5, temperature not specified in the publication
Streptomyces lividus
1.1.3.44
6.4
-
pH 7.5, temperature not specified in the publication
Streptomyces fradiae
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
1.1.3.43
paromamine + O2
-
719676
Streptomyces fradiae
6'-dehydro-paromamine + H2O2
-
-
-
?
1.1.3.43
paromamine + O2
-
719676
Streptomyces fradiae NCIMB 8233
6'-dehydro-paromamine + H2O2
-
-
-
?
1.1.3.44
2'''-N-acetyl-6'''-hydroxyneomycin C + O2
about 15% of the rate with 6'''-deamino-6'''-hydroxyneomycin C
719676
Streptomyces fradiae
2'''-N-acetyl-6'''-oxoneomycin C + H2O2
-
-
-
?
1.1.3.44
2'''-N-acetyl-6'''-hydroxyneomycin C + O2
less than 10% of the rate with 6'''-deamino-6'''-hydroxyneomycin C
719676
Streptomyces lividus
2'''-N-acetyl-6'''-oxoneomycin C + H2O2
-
-
-
?
1.1.3.44
2'''-N-acetyl-6'''-hydroxyneomycin C + O2
about 15% of the rate with 6'''-deamino-6'''-hydroxyneomycin C
719676
Streptomyces fradiae NCIMB 8233
2'''-N-acetyl-6'''-oxoneomycin C + H2O2
-
-
-
?
1.1.3.44
6'''-deamino-6'''-hydroxyneomycin C + O2
-
719676
Streptomyces fradiae
6'''-deamino-6'''-oxoneomycin C + H2O2
-
-
-
?
1.1.3.44
6'''-deamino-6'''-hydroxyneomycin C + O2
-
719676
Streptomyces lividus
6'''-deamino-6'''-oxoneomycin C + H2O2
-
-
-
?
1.1.3.44
6'''-deamino-6'''-hydroxyneomycin C + O2
-
719676
Streptomyces fradiae NCIMB 8233
6'''-deamino-6'''-oxoneomycin C + H2O2
-
-
-
?
1.1.3.44
additional information
enzyme does not catalyze the reaction of EC 1.1.3.43, paromamine 6'-oxidase
719676
Streptomyces lividus
?
-
-
-
?
2.6.1.93
6'-dehydroparomamine + L-glutamate
-
719676
Streptomyces fradiae
neamine + 2-oxoglutarate
-
-
-
?
2.6.1.95
additional information
NeoB is a bifunctional enzyme that also catalyses the NH2 group transfer at the 6'''-position
719676
Streptomyces fradiae
?
-
-
-
?
2.6.1.95
neomycin C + 2-oxoglutarate
-
719676
Streptomyces fradiae
6'''-hydroxyneomycin C + L-glutamate
-
-
-
?
Synonyms
EC Number
Synonyms
Commentary
Organism
1.1.3.43
neoQ
-
Streptomyces fradiae
1.1.3.44
LivQ
-
Streptomyces lividus
1.1.3.44
neoQ
-
Streptomyces fradiae
2.6.1.93
neoB
-
Streptomyces fradiae
2.6.1.95
neoB
-
Streptomyces fradiae
Application (protein specific)
EC Number
Application
Commentary
Organism
1.1.3.43
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
Streptomyces fradiae
1.1.3.44
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
Streptomyces lividus
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.1.3.43
expression in Escherichia coli
Streptomyces fradiae
1.1.3.44
expression in Escherichia coli
Streptomyces fradiae
1.1.3.44
expression in Escherichia coli
Streptomyces lividus
2.6.1.93
expressed in Escherichia coli
Streptomyces fradiae
2.6.1.95
expressed in Escherichia coli
Streptomyces fradiae
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.1.3.43
4.2
-
pH 7.5, temperature not specified in the publication
Streptomyces fradiae
1.1.3.44
3.5
-
pH 7.5, temperature not specified in the publication
Streptomyces lividus
1.1.3.44
6.4
-
pH 7.5, temperature not specified in the publication
Streptomyces fradiae
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
1.1.3.43
paromamine + O2
-
719676
Streptomyces fradiae
6'-dehydro-paromamine + H2O2
-
-
-
?
1.1.3.43
paromamine + O2
-
719676
Streptomyces fradiae NCIMB 8233
6'-dehydro-paromamine + H2O2
-
-
-
?
1.1.3.44
2'''-N-acetyl-6'''-hydroxyneomycin C + O2
about 15% of the rate with 6'''-deamino-6'''-hydroxyneomycin C
719676
Streptomyces fradiae
2'''-N-acetyl-6'''-oxoneomycin C + H2O2
-
-
-
?
1.1.3.44
2'''-N-acetyl-6'''-hydroxyneomycin C + O2
less than 10% of the rate with 6'''-deamino-6'''-hydroxyneomycin C
719676
Streptomyces lividus
2'''-N-acetyl-6'''-oxoneomycin C + H2O2
-
-
-
?
1.1.3.44
2'''-N-acetyl-6'''-hydroxyneomycin C + O2
about 15% of the rate with 6'''-deamino-6'''-hydroxyneomycin C
719676
Streptomyces fradiae NCIMB 8233
2'''-N-acetyl-6'''-oxoneomycin C + H2O2
-
-
-
?
1.1.3.44
6'''-deamino-6'''-hydroxyneomycin C + O2
-
719676
Streptomyces fradiae
6'''-deamino-6'''-oxoneomycin C + H2O2
-
-
-
?
1.1.3.44
6'''-deamino-6'''-hydroxyneomycin C + O2
-
719676
Streptomyces lividus
6'''-deamino-6'''-oxoneomycin C + H2O2
-
-
-
?
1.1.3.44
6'''-deamino-6'''-hydroxyneomycin C + O2
-
719676
Streptomyces fradiae NCIMB 8233
6'''-deamino-6'''-oxoneomycin C + H2O2
-
-
-
?
1.1.3.44
additional information
enzyme does not catalyze the reaction of EC 1.1.3.43, paromamine 6'-oxidase
719676
Streptomyces lividus
?
-
-
-
?
2.6.1.93
6'-dehydroparomamine + L-glutamate
-
719676
Streptomyces fradiae
neamine + 2-oxoglutarate
-
-
-
?
2.6.1.95
additional information
NeoB is a bifunctional enzyme that also catalyses the NH2 group transfer at the 6'''-position
719676
Streptomyces fradiae
?
-
-
-
?
2.6.1.95
neomycin C + 2-oxoglutarate
-
719676
Streptomyces fradiae
6'''-hydroxyneomycin C + L-glutamate
-
-
-
?