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show all sequences of 1.13.11.43

Reactivity and stability of lignostilbene-alpha,beta-dioxygenase-I in various pHs, temperatures, and in aqueous organic solvents

Makoto, N.; Kamoda, S.; Saburi, Y.; J. Microbiol. Biotechnol. 11, 884-886 (2001)
No PubMed abstract available

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
methanol
12fold activity increase by 30% methanol
Sphingomonas paucimobilis
Organic Solvent Stability
Organic Solvent
Commentary
Organism
Methanol
stable in 10% methanol, isozyme I
Sphingomonas paucimobilis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sphingomonas paucimobilis
-
four isoenzymes
-
Sphingomonas paucimobilis TMY 1009
-
four isoenzymes
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
isozyme I
Sphingomonas paucimobilis
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
-
stable, isozyme I
Sphingomonas paucimobilis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
isozyme I
Sphingomonas paucimobilis
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
methanol
12fold activity increase by 30% methanol
Sphingomonas paucimobilis
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
Methanol
stable in 10% methanol, isozyme I
Sphingomonas paucimobilis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
isozyme I
Sphingomonas paucimobilis
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
-
stable, isozyme I
Sphingomonas paucimobilis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
isozyme I
Sphingomonas paucimobilis
Other publictions for EC 1.13.11.43
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
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)
672665
Kamoda
Production of heterogeneous di ...
Sphingomonas paucimobilis, Sphingomonas paucimobilis TMY1009
Biosci. Biotechnol. Biochem.
69
635-637
2005
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
1
-
-
-
2
-
4
1
-
-
-
-
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-
-
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1
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-
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1
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2
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
655038
Kamoda
A common structure of substrat ...
Sphingomonas paucimobilis, Sphingomonas paucimobilis TMY1009
Biosci. Biotechnol. Biochem.
67
1394-1396
2003
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-
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1
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3
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6
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6
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656384
Han
N-benzylideneaniline and N-ben ...
Sphingomonas paucimobilis
J. Enzyme Inhib. Med. Chem.
18
279-283
2003
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-
-
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3
1
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1
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1
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440280
Makoto
-
Reactivity and stability of li ...
Sphingomonas paucimobilis, Sphingomonas paucimobilis TMY 1009
J. Microbiol. Biotechnol.
11
884-886
2001
1
-
-
-
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-
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1
7
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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
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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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-
-
440281
Kamoda
Purification and some properti ...
Sphingomonas paucimobilis, Sphingomonas paucimobilis TMY 1009
Biosci. Biotechnol. Biochem.
61
1575-1576
1997
-
-
-
-
-
-
-
2
-
-
2
-
-
7
-
-
1
-
-
-
-
-
4
1
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-
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2
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2
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1
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4
1
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-
-
-
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-
-
-
-
440282
Kamoda
Cloning of a lignostilbene-alp ...
Sphingomonas paucimobilis, Sphingomonas paucimobilis TMY 1009
Biosci. Biotechnol. Biochem.
59
1866-1868
1995
-
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1
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-
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1
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7
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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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2
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440283
Kamoda
Structural and enzymic compari ...
Sphingomonas paucimobilis, Sphingomonas paucimobilis TMY 1009
Biosci. Biotechnol. Biochem.
57
931-934
1993
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2
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7
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1
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8
2
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2
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1
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8
2
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440284
Kamoda
Cloning of a lignostilbene-alp ...
Sphingomonas paucimobilis, Sphingomonas paucimobilis TMY 1009
Agric. Biol. Chem.
55
1411-1412
1991
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1
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7
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440285
Kamoda
-
Purification and some properti ...
Sphingomonas paucimobilis, Sphingomonas paucimobilis TMY 1009
Agric. Biol. Chem.
53
2757-2761
1989
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2
1
1
2
2
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7
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1
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1
8
1
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1
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1
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2
1
1
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2
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1
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1
8
1
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1
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1
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