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Literature summary extracted from

  • 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 (2011), J. Appl. Microbiol., 111, 642-651.
    View publication on PubMed

Application

EC Number Application Comment 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 (Comment) 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 Comment 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] Comment 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.43 paromamine + O2
-
Streptomyces fradiae 6'-dehydro-paromamine + H2O2
-
?
1.1.3.43 paromamine + O2
-
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 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 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 Streptomyces fradiae NCIMB 8233 2'''-N-acetyl-6'''-oxoneomycin C + H2O2
-
?
1.1.3.44 6'''-deamino-6'''-hydroxyneomycin C + O2
-
Streptomyces fradiae 6'''-deamino-6'''-oxoneomycin C + H2O2
-
?
1.1.3.44 6'''-deamino-6'''-hydroxyneomycin C + O2
-
Streptomyces lividus 6'''-deamino-6'''-oxoneomycin C + H2O2
-
?
1.1.3.44 6'''-deamino-6'''-hydroxyneomycin C + O2
-
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 Streptomyces lividus ?
-
?
2.6.1.93 6'-dehydroparomamine + L-glutamate
-
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 Streptomyces fradiae ?
-
?
2.6.1.95 neomycin C + 2-oxoglutarate
-
Streptomyces fradiae 6'''-hydroxyneomycin C + L-glutamate
-
?

Synonyms

EC Number Synonyms Comment 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