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show all sequences of 1.1.9.1

Quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni. Purification, characterization, and reconstitution of the apoenzyme with pyrolloquinoline quinone analogues

De Jong, G.A.H.; Geerlof, A.; Stoorvogel, J.; Jongejan, J.A.; de Vries, S.; Duine, J.a.; Eur. J. Biochem. 230, 899-905 (1995)

Data extracted from this reference:

Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme
Comamonas testosteroni
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
71000
-
PAGE
Comamonas testosteroni
73200
-
1 * 71000, SDS-PAGE, 1 * 73200, calculated
Comamonas testosteroni
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Comamonas testosteroni
-
-
-
Purification (Commentary)
Commentary
Organism
from ethanol-grown cells
Comamonas testosteroni
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
20.5
-
-
Comamonas testosteroni
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
n-butanol + ferricyanide
-
389960
Comamonas testosteroni
butanal + ferrocyanide
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 71000, SDS-PAGE, 1 * 73200, calculated
Comamonas testosteroni
Cofactor
Cofactor
Commentary
Organism
Structure
heme
holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme. Low-spin heme protein
Comamonas testosteroni
pyrroloquinoline quinone
holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme. Reconstitution of apoenzyme with pyrroloquinoline quinone analogues results in a decreased activity and enantioselectivity for the oxidation of chiral alcohols. Possession of the o-quinone or o-quinol moiety is not essential for binding but it is for activity
Comamonas testosteroni
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
heme
holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme. Low-spin heme protein
Comamonas testosteroni
pyrroloquinoline quinone
holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme. Reconstitution of apoenzyme with pyrroloquinoline quinone analogues results in a decreased activity and enantioselectivity for the oxidation of chiral alcohols. Possession of the o-quinone or o-quinol moiety is not essential for binding but it is for activity
Comamonas testosteroni
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme
Comamonas testosteroni
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
71000
-
PAGE
Comamonas testosteroni
73200
-
1 * 71000, SDS-PAGE, 1 * 73200, calculated
Comamonas testosteroni
Purification (Commentary) (protein specific)
Commentary
Organism
from ethanol-grown cells
Comamonas testosteroni
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
20.5
-
-
Comamonas testosteroni
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
n-butanol + ferricyanide
-
389960
Comamonas testosteroni
butanal + ferrocyanide
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 71000, SDS-PAGE, 1 * 73200, calculated
Comamonas testosteroni
Other publictions for EC 1.1.9.1
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)
654868
Jongejan
Deuterium isotope effect on en ...
Comamonas testosteroni
Biochim. Biophys. Acta
1647
297-302
2003
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1
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1
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656080
Oubrie
Crystal structure of quinohemo ...
Comamonas testosteroni
J. Biol. Chem.
277
3727-3732
2002
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678768
Toyama
Azurin involved in alcohol oxi ...
Pseudomonas putida
Biosci. Biotechnol. Biochem.
65
1617-1626
2001
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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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1
1
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1
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701480
Oubrie
Crystallization of quinohemopr ...
Comamonas testosteroni
Acta Crystallogr. Sect. D
D57
1732-1734
2001
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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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701774
Somers
-
Enantioselective oxidation of ...
Comamonas testosteroni
Appl. Biochem. Biotechnol.
75
151-161
1999
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1
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50
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1
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35
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1
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50
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35
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705187
Stigter
-
Enantioselective oxidation of ...
Comamonas testosteroni
J. Mol. Catal. B
2
291-297
1997
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21
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22
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389956
De Jong
Characterization of the intera ...
Comamonas testosteroni
Biochemistry
34
9451-9458
1995
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2
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389960
De Jong
Quinohemoprotein ethanol dehyd ...
Comamonas testosteroni
Eur. J. Biochem.
230
899-905
1995
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1
2
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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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2
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1
2
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1
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1
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1
1
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687362
Toyama
Three distinct quinoprotein al ...
Pseudomonas putida
J. Bacteriol.
177
2442-2450
1995
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7
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26
1
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26
1
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1
1
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703526
Geerlof
Description of the kinetic mec ...
Comamonas testosteroni
Eur. J. Biochem.
226
537-546
1994
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6
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1
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7
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7
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6
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7
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7
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6
6
389953
Groen
Quinohaemoprotein alcohol dehy ...
Comamonas testosteroni
Biochem. J.
234
611-615
1986
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12
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2
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15
1
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1
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2
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12
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2
15
1
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1
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