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Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer

Oubrie, A.; Rozeboom, H.J.; Kalk, K.H.; Huizinga, E.G.; Dijkstra, B.W.; J. Biol. Chem. 277, 3727-3732 (2002)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
to 1.44 A resolution. The N-terminal domain has a beta-propeller fold and binds one pyrroloquinoline quinone cofactor and one calcium ion in the active site. A tetrahydrofuran-2-carboxylic acid molecule is present in the substrate-binding cleft. The C-terminal domain is an -helical type I cytochrome c with His608 and Met647 as heme-iron ligands. An unusual disulfide bond between two adjacent cysteines bridges the redox centers. It appears essential for electron transfer. A water channel delineates a possible pathway for proton transfer from the active site to the solvent
Comamonas testosteroni
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Comamonas testosteroni
Q46444
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Crystallization (Commentary) (protein specific)
Crystallization
Organism
to 1.44 A resolution. The N-terminal domain has a beta-propeller fold and binds one pyrroloquinoline quinone cofactor and one calcium ion in the active site. A tetrahydrofuran-2-carboxylic acid molecule is present in the substrate-binding cleft. The C-terminal domain is an -helical type I cytochrome c with His608 and Met647 as heme-iron ligands. An unusual disulfide bond between two adjacent cysteines bridges the redox centers. It appears essential for electron transfer. A water channel delineates a possible pathway for proton transfer from the active site to the solvent
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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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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701480
Oubrie
Crystallization of quinohemopr ...
Comamonas testosteroni
Acta Crystallogr. Sect. D
D57
1732-1734
2001
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701774
Somers
-
Enantioselective oxidation of ...
Comamonas testosteroni
Appl. Biochem. Biotechnol.
75
151-161
1999
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705187
Stigter
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Enantioselective oxidation of ...
Comamonas testosteroni
J. Mol. Catal. B
2
291-297
1997
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389956
De Jong
Characterization of the intera ...
Comamonas testosteroni
Biochemistry
34
9451-9458
1995
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389960
De Jong
Quinohemoprotein ethanol dehyd ...
Comamonas testosteroni
Eur. J. Biochem.
230
899-905
1995
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687362
Toyama
Three distinct quinoprotein al ...
Pseudomonas putida
J. Bacteriol.
177
2442-2450
1995
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703526
Geerlof
Description of the kinetic mec ...
Comamonas testosteroni
Eur. J. Biochem.
226
537-546
1994
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389953
Groen
Quinohaemoprotein alcohol dehy ...
Comamonas testosteroni
Biochem. J.
234
611-615
1986
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