BRENDA - Enzyme Database show
show all sequences of 1.1.1.30

Molecular basis of substrate recognition in D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida

Feller, C.; Guenther, R.; Hofmann, H.J.; Grunow, M.; ChemBioChem 7, 1410-1418 (2006)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Pseudomonas putida
Engineering
Amino acid exchange
Commentary
Organism
H141A
kcat/KM for (R)-3-hydroxybutanoate is 184.2fold lower than wild-type value, kcat/Km for NAD+ is 12.9fold lower than wild-type enzyme
Pseudomonas putida
K149A
inactive mutant enzyme
Pseudomonas putida
K149R
kcat/KM for (R)-3-hydroxybutanoate is 184.2fold lower than wild-type value, kcat/Km for NAD+ is 7.2fold lower than wild-type enzyme
Pseudomonas putida
Q193A
kcat/KM for (R)-3-hydroxybutanoate is 307fold lower than wild-type value, kcat/Km for NAD+ is 6.2fold lower than wild-type enzyme
Pseudomonas putida
Q91A
kcat/KM for (R)-3-hydroxybutanoate is 83.7fold lower than wild-type value, kcat/Km for NAD+ is 2.8fold lower than wild-type enzyme
Pseudomonas putida
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.18
-
NAD+
23C, pH 8.0, wild-type enzyme
Pseudomonas putida
0.27
-
NAD+
23C, pH 8.0, mutant enzyme Q193A
Pseudomonas putida
0.28
-
NAD+
23C, pH 8.0, mutant enzyme H141A
Pseudomonas putida
0.38
-
NAD+
23C, pH 8.0, mutant enzyme K149R
Pseudomonas putida
0.51
-
NAD+
23C, pH 8.0, mutant enzyme Q91A
Pseudomonas putida
1.5
-
(R)-3-hydroxybutanoate
23C, pH 8.0, wild-type enzyme
Pseudomonas putida
35
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme H141A
Pseudomonas putida
78
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme K149R
Pseudomonas putida
96
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme Q193A
Pseudomonas putida
131
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme Q91A
Pseudomonas putida
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
Q9AE70
-
-
Purification (Commentary)
Commentary
Organism
-
Pseudomonas putida
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-3-hydroxybutanoate + NAD+
-
668251
Pseudomonas putida
acetoacetate + NADH + H+
-
-
-
r
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
167
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme H141A
Pseudomonas putida
333
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme Q193A
Pseudomonas putida
404
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme K149R
Pseudomonas putida
1382
-
(R)-3-hydroxybutanoate
23C, pH 8.0, wild-type enzyme
Pseudomonas putida
1390
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme Q91A
Pseudomonas putida
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Pseudomonas putida
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Pseudomonas putida
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Pseudomonas putida
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
H141A
kcat/KM for (R)-3-hydroxybutanoate is 184.2fold lower than wild-type value, kcat/Km for NAD+ is 12.9fold lower than wild-type enzyme
Pseudomonas putida
K149A
inactive mutant enzyme
Pseudomonas putida
K149R
kcat/KM for (R)-3-hydroxybutanoate is 184.2fold lower than wild-type value, kcat/Km for NAD+ is 7.2fold lower than wild-type enzyme
Pseudomonas putida
Q193A
kcat/KM for (R)-3-hydroxybutanoate is 307fold lower than wild-type value, kcat/Km for NAD+ is 6.2fold lower than wild-type enzyme
Pseudomonas putida
Q91A
kcat/KM for (R)-3-hydroxybutanoate is 83.7fold lower than wild-type value, kcat/Km for NAD+ is 2.8fold lower than wild-type enzyme
Pseudomonas putida
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.18
-
NAD+
23C, pH 8.0, wild-type enzyme
Pseudomonas putida
0.27
-
NAD+
23C, pH 8.0, mutant enzyme Q193A
Pseudomonas putida
0.28
-
NAD+
23C, pH 8.0, mutant enzyme H141A
Pseudomonas putida
0.38
-
NAD+
23C, pH 8.0, mutant enzyme K149R
Pseudomonas putida
0.51
-
NAD+
23C, pH 8.0, mutant enzyme Q91A
Pseudomonas putida
1.5
-
(R)-3-hydroxybutanoate
23C, pH 8.0, wild-type enzyme
Pseudomonas putida
35
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme H141A
Pseudomonas putida
78
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme K149R
Pseudomonas putida
96
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme Q193A
Pseudomonas putida
131
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme Q91A
Pseudomonas putida
Purification (Commentary) (protein specific)
Commentary
Organism
-
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-3-hydroxybutanoate + NAD+
-
668251
Pseudomonas putida
acetoacetate + NADH + H+
-
-
-
r
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
167
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme H141A
Pseudomonas putida
333
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme Q193A
Pseudomonas putida
404
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme K149R
Pseudomonas putida
1382
-
(R)-3-hydroxybutanoate
23C, pH 8.0, wild-type enzyme
Pseudomonas putida
1390
-
(R)-3-hydroxybutanoate
23C, pH 8.0, mutant enzyme Q91A
Pseudomonas putida
Other publictions for EC 1.1.1.30
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)
737394
Kanazawa
Structural insights into the c ...
Alcaligenes faecalis
Acta Crystallogr. Sect. F
72
507-515
2016
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1
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1
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737914
Yeon
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Structural basis for the subst ...
Alcaligenes faecalis
Biotechnol. Bioprocess Eng.
21
364-372
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-
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1
-
15
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15
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1
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1
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1
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2
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15
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1
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1
1
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15
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15
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1
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1
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2
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15
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13
13
739558
Davuluri
Inactivation of 3-hydroxybutyr ...
Danio rerio
Proc. Natl. Acad. Sci. USA
113
E1460-E1469
2016
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1
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1
1
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737467
Scaturro
Identification and characteriz ...
Legionella pneumophila subsp. pneumophila, Legionella pneumophila subsp. pneumophila DSM 7513
APMIS
123
330-341
2015
-
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1
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2
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6
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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
1
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1
-
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-
-
-
729048
Lu
3-Hydroxybutyrate oligomer hyd ...
Paracoccus denitrificans, Paracoccus denitrificans ATCC 17741
Appl. Environ. Microbiol.
80
986-993
2014
-
-
1
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1
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1
2
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4
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1
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1
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4
1
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737912
Yeon
-
Effect of His-tag location on ...
Alcaligenes faecalis
Biotechnol. Bioprocess Eng.
19
798-802
2014
-
-
1
-
3
2
-
8
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1
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1
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2
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8
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1
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1
1
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3
2
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8
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1
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2
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8
-
-
-
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8
8
738207
Liu
3-Hydroxybutyrate dehydrogenas ...
Mus musculus
FEBS J.
281
2410-2421
2014
-
-
-
-
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-
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4
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1
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1
1
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-
721853
Yeon
Enzymatic reduction of levulin ...
Alcaligenes faecalis
Biores. Technol.
134
377-380
2013
-
1
1
-
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
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
1
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-
711807
Mountassif
Structural and catalytic prope ...
Pseudomonas aeruginosa
Curr. Microbiol.
61
7-12
2010
-
-
1
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1
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3
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2
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695376
Hoque
Structure of D-3-hydroxybutyra ...
Alcaligenes faecalis
Acta Crystallogr. Sect. F
65
331-335
2009
-
-
1
1
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1
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695653
Takanashi
Characterization of a novel 3- ...
Ralstonia pickettii, Ralstonia pickettii T1
Antonie van Leeuwenhoek
95
249-262
2009
1
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1
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1
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12
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9
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12
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12
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1
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12
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1
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698660
Nakashima
Closed complex of the D-3-hydr ...
Pseudomonas fragi
J. Biochem.
145
467-479
2009
-
-
1
1
22
-
1
47
-
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2
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1
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1
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24
1
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1
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22
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1
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47
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1
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24
1
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684149
Hoque
The structures of Alcaligenes ...
Alcaligenes faecalis
Acta Crystallogr. Sect. D
64
496-505
2008
-
1
1
1
-
-
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1
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2
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1
1
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689351
Mountassif
-
Biochemical and histological a ...
Jaculus orientalis
Pestic. Biochem. Physiol.
90
87-96
2008
-
-
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1
2
1
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1
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1
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679792
Paithankar
Cosubstrate-induced dynamics o ...
Pseudomonas putida
FEBS J.
274
5767-5779
2007
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1
1
4
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4
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4
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1
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2
4
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1
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4
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680512
Uchino
Isolated poly(3-hydroxybutyrat ...
Cupriavidus necator
J. Bacteriol.
189
8250-8256
2007
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1
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1
3
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1
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1
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685409
Mountassif
Prehibernation and hibernation ...
Jaculus orientalis
Biochimie
89
1019-1028
2007
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1
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2
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1
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1
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2
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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
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2
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1
-
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2
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2
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1
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668251
Feller
Molecular basis of substrate r ...
Pseudomonas putida
ChemBioChem
7
1410-1418
2006
-
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1
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5
-
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10
-
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-
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2
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1
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-
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1
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-
-
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5
-
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1
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1
1
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5
-
-
-
-
10
-
-
-
-
-
-
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1
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1
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5
-
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668322
Mountassif
-
Characterization of two D-b-hy ...
Jaculus orientalis
Comp. Biochem. Physiol. B
143B
285-293
2006
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2
4
1
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1
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1
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3
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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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4
1
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Characterization of human DHRS ...
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J. Biol. Chem.
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Takanashi
Characterization of two 3-hydr ...
Ralstonia pickettii, Ralstonia pickettii T1
J. Biosci. Bioeng.
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2
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669873
Ito
D-3-hydroxybutyrate dehydrogen ...
Pseudomonas fragi
J. Mol. Biol.
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2006
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667070
Nakajima
Crystallization and preliminar ...
Pseudomonas fragi
Acta Crystallogr. Sect. F
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656326
Takanashi
Biochemical and genetic charac ...
Acidovorax sp.
J. Biosci. Bioeng.
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78-81
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655126
Kabine
Hibernation impact on the cata ...
Jaculus orientalis
BMC Biochem.
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9
2
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9
2
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3
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1
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1
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655261
Nasser
Purification and characterizat ...
Camelus dromedarius
Comp. Biochem. Physiol. B
131
9-18
2002
1
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3
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1
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2
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286512
Loeb-Hennard
-
(R)-3-Hydroxybutyrate dehydrog ...
Homo sapiens
Biochemistry
39
11929-11938
2000
1
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1
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2
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1
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286513
Green
Wild type and mutant human hea ...
Bos taurus, Homo sapiens
Biochemistry
35
8158-8165
1996
2
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1
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3
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6
4
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7
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2
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286514
Klein
Specific interaction of(R)-3-h ...
Bos taurus
Biochemistry
35
3044-3049
1996
1
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2
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1
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286515
Szewczyk
Occurence, purification and pr ...
Staphylococcus xylosus
Acta Microbiol. Pol.
43
33-45
1994
1
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4
2
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6
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1
1
1
1
1
1
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1
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286516
Adam
Monoclonal antibodies for stru ...
Bos taurus, Rattus norvegicus
Biochem. J.
292
863-872
1993
2
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4
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2
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286517
Dalton
Effect of selective thiol-grou ...
Bos taurus
Biochem. J.
296
563-569
1993
1
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1
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286518
Dutra
Inhibition of succinate dehydr ...
Rattus norvegicus
J. Inherit. Metab. Dis.
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147-153
1993
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4
2
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1
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286519
Marks
Molecular cloning and characte ...
Homo sapiens
J. Biol. Chem.
267
15459-15463
1992
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1
1
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-
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286520
Bailly
Post-transcriptional analysis ...
Rattus norvegicus
Biol. Cell.
73
121-129
1991
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3
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1
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-
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-
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286521
McIntyre
Comparison of 3-hydroxybutyrat ...
Bos taurus, Rattus norvegicus
Arch. Biochem. Biophys.
262
85-98
1988
2
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-
-
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4
4
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4
2
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4
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2
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7
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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4
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2
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7
2
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2
2
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-
-
-
-
-
-
-
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286522
Cortese
Noncooperative vs. cooperative ...
Bos taurus, Rattus norvegicus
Biochemistry
26
5283-5293
1987
2
-
-
-
-
-
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2
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2
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3
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2
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-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286523
Worral
3-Hydroxyisobutyrate dehydroge ...
Rhodobacter sphaeroides
Biochem. J.
241
297-300
1987
1
-
-
-
-
-
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1
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1
-
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1
-
1
-
-
-
-
-
-
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-
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286524
Kovar
-
Kinetics of D-3-hydroxybutyrat ...
Paracoccus denitrificans
Biochim. Biophys. Acta
871
302-309
1986
1
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7
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7
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1
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-
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-
-
2
-
-
-
-
-
-
-
-
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286525
Dubois
Cyanylation of 3-hydroxybutyra ...
Bos taurus
Biol. Chem. Hoppe-Seyler
367
343-353
1986
1
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-
-
-
-
2
8
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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286526
Matyskova I.; Kovar
-
Purification and properties of ...
Paracoccus denitrificans
Biochim. Biophys. Acta
839
300-307
1985
1
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1
1
1
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1
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1
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1
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2
1
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1
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1
1
1
1
-
-
-
-
-
-
-
-
-
-
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286527
Burnett
A rapid and efficient procedur ...
Bos taurus
Biochim. Biophys. Acta
815
51-56
1985
1
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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
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-
-
-
-
-
-
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286529
MacGill
-
D-3-Hydroxybutyrate dehydrogen ...
Rattus norvegicus
Biochem. Soc. Trans.
607
788
1984
1
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1
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1
1
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1
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-
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286530
McIntyre
Target size of D-beta-hydroxyb ...
Bos taurus
J. Biol. Chem.
258
953-959
1983
1
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1
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1
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-
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-
-
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286531
Scawen
The rapid purification of 3-hy ...
Rhodobacter sphaeroides
Biochem. J.
203
699-705
1982
1
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1
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1
1
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-
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-
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286528
Phelps
Inhibition of D(-)-beta-hydrox ...
Bos taurus
Biochemistry
20
459-463
1981
1
-
-
-
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4
1
1
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1
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1
1
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2
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-
-
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286532
Kluger
Inhibition of bacterial D-3-hy ...
Paucimonas lemoignei
Can. J. Biochem.
59
810-815
1981
1
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8
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8
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1
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286533
Miyahara
Selective interaction of D-bet ...
Rattus norvegicus
Biochim. Biophys. Acta
641
222-231
1981
1
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286534
Nakada T.; Fukui
Purification and properties of ...
Zoogloea ramigera I-16-M
J. Biochem.
89
625-635
1981
6
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1
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6
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1
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17
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4
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2
2
1
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1
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1
1
1
1
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-
-
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1
1
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-
-
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286535
Phelps
Inhibition of D(-)-beta-hydrox ...
Bos taurus
Biochemistry
20
453-458
1981
1
-
-
-
-
-
6
4
1
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-
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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1
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1
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6
-
4
1
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1
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1
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1
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286536
Tucker
The kinetics of rat liver and ...
Rattus norvegicus
Biochem. J.
179
579-581
1979
1
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8
1
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1
-
3
-
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-
-
-
4
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1
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1
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1
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1
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8
1
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1
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4
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1
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-
-
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-
-
-
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-
286537
Kluger
-
Substrate analogue studies of ...
Paucimonas lemoignei
J. Am. Chem. Soc.
100
7388-7392
1978
1
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-
-
10
-
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1
-
1
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3
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1
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1
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1
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1
-
-
-
-
10
-
-
-
-
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1
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-
-
-
-
-
-
-
3
-
-
-
-
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1
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-
-
-
-
-
-
-
-
286538
McIntyre
The orientation of D-beta-hydr ...
Bos taurus
Biochim. Biophys. Acta
513
255-267
1978
1
-
-
-
-
-
-
-
2
-
-
1
-
2
-
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-
-
2
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
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1
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2
1
-
1
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-
286539
Dhariwal
Purification and properties of ...
Mycobacterium phlei
J. Gen. Microbiol.
104
123-126
1978
1
-
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-
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2
2
-
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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
-
2
1
-
1
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-
1
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1
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2
-
2
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1
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1
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1
-
1
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-
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1
-
2
1
-
-
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-
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-
-
-
286540
Tan
Inhibition of D(-)-3-hydroxybu ...
Bos taurus, Cavia porcellus, Rattus norvegicus
Arch. Biochem. Biophys.
166
164-173
1975
3
-
-
-
-
-
20
-
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3
-
3
-
-
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-
-
3
-
-
3
-
-
-
-
-
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3
-
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3
-
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3
-
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-
-
20
-
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3
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3
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3
-
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286541
Thompson
Characterization and partial p ...
Bacillus cereus, Bacillus cereus T
Can. J. Microbiol.
19
673-677
1973
1
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2
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1
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2
-
8
-
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1
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1
1
2
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1
1
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1
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1
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1
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-
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2
-
1
-
2
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1
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1
1
2
-
-
-
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1
1
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-
-
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-
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-
286542
Nielsen
Mitochondrial D-beta-hydroxybu ...
Bos taurus
J. Biol. Chem.
248
2549-2555
1973
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
1
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1
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-
-
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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
1
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1
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-
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286543
Nielsen
Mitochondrial D-beta-hydroxybu ...
Bos taurus
J. Biol. Chem.
248
2556-2562
1973
1
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-
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5
-
-
-
-
1
-
1
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-
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-
-
-
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1
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-
-
-
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-
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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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