BRENDA - Enzyme Database
show all sequences of 1.1.3.44

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
Application
Commentary
Organism
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)
Cloned (Commentary)
Organism
expression in Escherichia coli
Streptomyces fradiae
expression in Escherichia coli
Streptomyces lividus
Organism
Organism
UniProt
Commentary
Textmining
Streptomyces fradiae
Q53U15
-
-
Streptomyces fradiae NCIMB 8233
Q53U15
-
-
Streptomyces lividus
Q2MF66
-
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
3.5
-
pH 7.5, temperature not specified in the publication
Streptomyces lividus
6.4
-
pH 7.5, temperature not specified in the publication
Streptomyces fradiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
6'''-deamino-6'''-hydroxyneomycin C + O2
-
719676
Streptomyces fradiae
6'''-deamino-6'''-oxoneomycin C + H2O2
-
-
-
?
6'''-deamino-6'''-hydroxyneomycin C + O2
-
719676
Streptomyces lividus
6'''-deamino-6'''-oxoneomycin C + H2O2
-
-
-
?
6'''-deamino-6'''-hydroxyneomycin C + O2
-
719676
Streptomyces fradiae NCIMB 8233
6'''-deamino-6'''-oxoneomycin C + H2O2
-
-
-
?
additional information
enzyme does not catalyze the reaction of EC 1.1.3.43, paromamine 6'-oxidase
719676
Streptomyces lividus
?
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
LivQ
-
Streptomyces lividus
neoQ
-
Streptomyces fradiae
Application (protein specific)
Application
Commentary
Organism
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)
Commentary
Organism
expression in Escherichia coli
Streptomyces fradiae
expression in Escherichia coli
Streptomyces lividus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
3.5
-
pH 7.5, temperature not specified in the publication
Streptomyces lividus
6.4
-
pH 7.5, temperature not specified in the publication
Streptomyces fradiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
6'''-deamino-6'''-hydroxyneomycin C + O2
-
719676
Streptomyces fradiae
6'''-deamino-6'''-oxoneomycin C + H2O2
-
-
-
?
6'''-deamino-6'''-hydroxyneomycin C + O2
-
719676
Streptomyces lividus
6'''-deamino-6'''-oxoneomycin C + H2O2
-
-
-
?
6'''-deamino-6'''-hydroxyneomycin C + O2
-
719676
Streptomyces fradiae NCIMB 8233
6'''-deamino-6'''-oxoneomycin C + H2O2
-
-
-
?
additional information
enzyme does not catalyze the reaction of EC 1.1.3.43, paromamine 6'-oxidase
719676
Streptomyces lividus
?
-
-
-
?
Other publictions for EC 1.1.3.44
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [░C]
Temperature Range [░C]
Temperature Stability [░C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [░C] (protein specific)
Temperature Range [░C] (protein specific)
Temperature Stability [░C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
719676
Clausnitzer
The oxidoreductases LivQ and N ...
Streptomyces lividus, Streptomyces fradiae, Streptomyces fradiae NCIMB 8233
J. Appl. Microbiol.
111
642-651
2011
-
1
2
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
2
-
7
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
719294
Huang
Elaboration of neosamine rings ...
Streptomyces fradiae, Streptomyces fradiae NCIMB 8233
ChemBioChem
8
283-288
2007
-
-
1
-
-
-
-
-
-
-
1
-
-
6
-
-
-
-
-
-
-
-
4
1
1
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
4
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-