BRENDA - Enzyme Database
show all sequences of 1.1.2.B5

pH-dependent electron transfer reaction and direct bioelectrocatalysis of the quinohemoprotein pyranose dehydrogenase

Takeda, K.; Matsumura, H.; Ishida, T.; Yoshida, M.; Igarashi, K.; Samejima, M.; Ohno, H.; Nakamura, N.; Biochem. Biophys. Res. Commun. 477, 369-373 (2016)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.3
-
ferricytochrome c
at pH 6.0 and 30C
Coprinopsis cinerea
6.1
-
ferricytochrome c
at pH 8.5 and 30C
Coprinopsis cinerea
Organism
Organism
UniProt
Commentary
Textmining
Coprinopsis cinerea
-
formally known as Coprinus cinereus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
L-fucose + ferricytochrome c
-
739998
Coprinopsis cinerea
2-dehydro-L-fucose + ferrocytochrome c
-
-
-
?
L-fucose + phenazine methosulfate
-
739998
Coprinopsis cinerea
2-dehydro-L-fucose + reduced phenazine methosulfate
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
PDH
-
Coprinopsis cinerea
quinohemoprotein pyranose dehydrogenase
-
Coprinopsis cinerea
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
30.7
-
ferricytochrome c
at pH 6.0 and 30C
Coprinopsis cinerea
53.5
-
ferricytochrome c
at pH 8.5 and 30C
Coprinopsis cinerea
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
for reduction of phenazine methosulfate
Coprinopsis cinerea
8.5
-
for reduction of ferricytochrome c
Coprinopsis cinerea
Cofactor
Cofactor
Commentary
Organism
Structure
heme b
-
Coprinopsis cinerea
pyrroloquinoline quinone
-
Coprinopsis cinerea
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
heme b
-
Coprinopsis cinerea
pyrroloquinoline quinone
-
Coprinopsis cinerea
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.3
-
ferricytochrome c
at pH 6.0 and 30C
Coprinopsis cinerea
6.1
-
ferricytochrome c
at pH 8.5 and 30C
Coprinopsis cinerea
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
L-fucose + ferricytochrome c
-
739998
Coprinopsis cinerea
2-dehydro-L-fucose + ferrocytochrome c
-
-
-
?
L-fucose + phenazine methosulfate
-
739998
Coprinopsis cinerea
2-dehydro-L-fucose + reduced phenazine methosulfate
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
30.7
-
ferricytochrome c
at pH 6.0 and 30C
Coprinopsis cinerea
53.5
-
ferricytochrome c
at pH 8.5 and 30C
Coprinopsis cinerea
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
for reduction of phenazine methosulfate
Coprinopsis cinerea
8.5
-
for reduction of ferricytochrome c
Coprinopsis cinerea
Other publictions for EC 1.1.2.B5
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)
739998
Takeda
pH-dependent electron transfer ...
Coprinopsis cinerea
Biochem. Biophys. Res. Commun.
477
369-373
2016
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2
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4
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2
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2
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2
2
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2
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2
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2
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2
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2
2
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741228
Takeda
Characterization of a novel PQ ...
Coprinopsis cinerea
PLoS ONE
10
e0115722
2015
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1
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9
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1
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7
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13
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2
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9
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2
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1
2
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9
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1
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13
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9
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9
9