BRENDA - Enzyme Database
show all sequences of 1.10.3.6

Transformation of rifamycin B with immobilized rifamycin oxidase of Curvularia lunata

Banerjee, U.C.; Biotechnol. Tech. 7, 339-344 (1993)

Data extracted from this reference:

General Stability
General Stability
Organism
increase by immobilization on polyacrylamide gel
Curvularia lunata
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
-
Curvularia lunata
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
rifamycin B + O2
Curvularia lunata
-
rifamycin O + H2O2
-
Curvularia lunata
?
Organism
Organism
UniProt
Commentary
Textmining
Curvularia lunata
-
MTCC 165
-
Reaction
Reaction
Commentary
Organism
Reaction ID
rifamycin B + O2 = rifamycin O + H2O2
immobilized enzyme
Curvularia lunata
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
rifamycin B + O2
-
439886
Curvularia lunata
rifamycin O + H2O2
-
439886
Curvularia lunata
?
rifamycin B + O2
-
439886
Curvularia lunata
rifamycin S + H2O2
-
439886
Curvularia lunata
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
immobilized enzyme
Curvularia lunata
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
30
60
activity is studied in this range
Curvularia lunata
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
immobilized enzyme has longer half life compared to free enzyme at 30°C and 40°C, the immobilized enzyme is more stable at higher temperatures
Curvularia lunata
30
-
immobilized enzyme has a half life time of 30 days
Curvularia lunata
50
-
immobilized enzyme has a half life time of 11.5 days
Curvularia lunata
60
-
soluble enzyme loses 80%, immobilized enzyme 50% of its maximum activity
Curvularia lunata
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
immobilized cells and soluble enzyme
Curvularia lunata
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5
8
activity is studied in this range, above pH 7.0 the activity is reduced dramatically
Curvularia lunata
General Stability (protein specific)
General Stability
Organism
increase by immobilization on polyacrylamide gel
Curvularia lunata
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
-
Curvularia lunata
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
rifamycin B + O2
Curvularia lunata
-
rifamycin O + H2O2
-
Curvularia lunata
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
rifamycin B + O2
-
439886
Curvularia lunata
rifamycin O + H2O2
-
439886
Curvularia lunata
?
rifamycin B + O2
-
439886
Curvularia lunata
rifamycin S + H2O2
-
439886
Curvularia lunata
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
immobilized enzyme
Curvularia lunata
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
30
60
activity is studied in this range
Curvularia lunata
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
immobilized enzyme has longer half life compared to free enzyme at 30°C and 40°C, the immobilized enzyme is more stable at higher temperatures
Curvularia lunata
30
-
immobilized enzyme has a half life time of 30 days
Curvularia lunata
50
-
immobilized enzyme has a half life time of 11.5 days
Curvularia lunata
60
-
soluble enzyme loses 80%, immobilized enzyme 50% of its maximum activity
Curvularia lunata
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
immobilized cells and soluble enzyme
Curvularia lunata
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5
8
activity is studied in this range, above pH 7.0 the activity is reduced dramatically
Curvularia lunata
Other publictions for EC 1.10.3.6
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)
688670
Jobanputra
-
Influence of nitrogen sources ...
Chryseobacterium sp.
J. Sci. Ind. Res.
66
615-617
2007
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-
-
-
-
-
-
-
-
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1
-
-
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1
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1
-
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-
-
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-
-
-
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-
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-
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-
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-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439887
Patil
-
Influence of substrate prepara ...
Curvularia lunata
Indian J. Exp. Biol.
35
917-919
1997
-
1
-
-
-
-
-
-
-
-
-
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3
1
-
-
-
-
-
-
-
-
1
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1
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1
-
-
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-
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1
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-
-
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-
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3
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
439886
Banerjee
Transformation of rifamycin B ...
Curvularia lunata
Biotechnol. Tech.
7
339-344
1993
-
-
-
-
-
1
-
-
1
-
-
1
-
1
-
-
-
1
-
-
-
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2
-
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1
1
4
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1
1
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-
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-
-
1
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-
-
-
1
-
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1
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-
-
-
-
-
-
2
-
1
1
4
-
1
1
-
-
-
-
-
-
-
-
439888
Banerjee
Characterization of soluble ri ...
Curvularia lunata
Lett. Appl. Microbiol.
17
1-3
1993
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1
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-
-
-
5
1
1
1
-
1
-
7
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1
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1
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1
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2
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1
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-
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1
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5
-
1
1
1
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1
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1
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1
-
1
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2
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1
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-
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-
-
-
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439883
Vohra
-
Microbial transformation of ri ...
Curvularia lunata
Biotechnol. Lett.
11
851-854
1989
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1
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-
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1
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1
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1
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1
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1
1
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1
1
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-
1
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-
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1
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1
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1
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1
1
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-
1
1
-
-
-
-
-
-
-
-
439884
Seong
-
Enzymatic oxidation of rifamyc ...
Humicola spp.
J. Ferment. Technol.
63
515-522
1985
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1
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-
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3
1
1
1
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1
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1
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1
1
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1
6
-
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1
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1
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1
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3
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1
1
1
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1
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1
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1
6
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1
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-
1
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-
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-
-
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439885
Lee
-
The properties of immobilized ...
Humicola spp.
Biotechnol. Lett.
6
143-148
1984
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1
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1
2
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1
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1
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1
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1
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2
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1
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1
1
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1
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1
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1
1
2
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1
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-
1
-
2
-
1
-
1
1
-
-
-
-
-
-
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-
439882
Han
Rifamycin B oxidase from Monoc ...
Monocillium spp.
FEBS Lett.
151
36-40
1983
1
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2
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1
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4
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1
1
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1
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5
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1
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1
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1
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1
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1
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2
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1
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1
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1
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5
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1
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1
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