BRENDA - Enzyme Database show
show all sequences of 1.1.1.30

Closed complex of the D-3-hydroxybutyrate dehydrogenase induced by an enantiomeric competitive inhibitor

Nakashima, K.; Ito, K.; Nakajima, Y.; Yamazawa, R.; Miyakawa, S.; Yoshimoto, T.; J. Biochem. 145, 467-479 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
wild-type and mutants expressed in Escherichia coli XL1Blue harbouring pHBDH11. Wild-type HBDH and mutants containing an N-terminal His-tag expressed in Escherichia coli XL1Blue using pQE30 as a vector
Pseudomonas fragi
Crystallization (Commentary)
Crystallization
Organism
crystals of ternary complex of HBDH-NAD+-L-3-hydroxybutyrate and the binary complex of HBDH-NAD+. The former structure shows a closed-form conformation, which is considered an active form for catalysis, while the latter stays mostly in a open-form conformation. Crystals of mutants T190S and T190A
Pseudomonas fragi
Engineering
Amino acid exchange
Commentary
Organism
H144A
catalytic efficiency (kcat/Km) is 0.2% of the activity of wild-type HBDH
Pseudomonas fragi
K152A
no activity
Pseudomonas fragi
K152E
very low activity
Pseudomonas fragi
K152Q
very low activity
Pseudomonas fragi
K152R
retains a significant level of activity
Pseudomonas fragi
L215A
both Km and kcat values are largely affected and the catalytic efficiency (kcat/Km) is less than 3% that of the wild-type enzyme
Pseudomonas fragi
L215V
Km values increase 3.5- and 4.3fold and the kcat values are 73-118% those of the wild-type toward D-3-hydroxybutyrate and acetoacetate, respectively. Mutation does not significantly change Km and kcat toward NAD+ and NADH
Pseudomonas fragi
Q196A
kcat/Km value is 0.6% that of the wild-type
Pseudomonas fragi
Q196E
substantially reduced activity
Pseudomonas fragi
Q196N
substantially reduced activity
Pseudomonas fragi
Q94A
catalytic efficiency (kcat/Km) is 1.4% of the activity of wild-type HBDH
Pseudomonas fragi
T190A
activity decreases to 0.1% that of the wild-type enzyme
Pseudomonas fragi
T190C
decreased activity
Pseudomonas fragi
T190S
retains 37% of the activity
Pseudomonas fragi
W187A
very low activity
Pseudomonas fragi
W187F
shows significant activity levels, 65% that of the wild-type enzyme
Pseudomonas fragi
W187T
shows faint activity
Pseudomonas fragi
W187Y
shows significant activity levels, 41% that of the wild-type enzyme
Pseudomonas fragi
W257A
no activity
Pseudomonas fragi
W257F
shows low activity levels, 2% that of the wild-type enzyme
Pseudomonas fragi
W257Y
shows low activity levels, 1% that of the wild-type enzyme
Pseudomonas fragi
Y155F
no activity
Pseudomonas fragi
Inhibitors
Inhibitors
Commentary
Organism
Structure
L-3-hydroxybutyrate
is a competitive inhibitor
Pseudomonas fragi
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
NADH
wild-type
Pseudomonas fragi
0.02
-
NADH
mutant T190S
Pseudomonas fragi
0.03
-
NADH
mutant L215V
Pseudomonas fragi
0.1
-
NADH
mutant T190A
Pseudomonas fragi
0.12
-
NAD+
mutant H6-K152R; mutant H6-Q196A; mutant H6-Q196E
Pseudomonas fragi
0.17
-
NAD+
H6-HBDH
Pseudomonas fragi
0.19
-
NAD+
mutant H6-Q94A
Pseudomonas fragi
0.2
-
NAD+
mutant H6-Q196N
Pseudomonas fragi
0.21
-
NAD+
mutant H6-W187Y
Pseudomonas fragi
0.24
-
NAD+
mutant H6-W187F; wild-type
Pseudomonas fragi
0.29
-
NAD+
mutant L215V
Pseudomonas fragi
0.35
-
NAD+
mutant H6-H144A
Pseudomonas fragi
0.37
-
acetoacetate
wild-type
Pseudomonas fragi
0.49
-
NAD+
mutant H6-W257F
Pseudomonas fragi
0.5
-
NADH
mutant L215A
Pseudomonas fragi
0.69
-
NAD+
mutant T190C
Pseudomonas fragi
0.71
-
NAD+
mutant T190S
Pseudomonas fragi
0.74
-
NAD+
mutant H6-W257Y
Pseudomonas fragi
0.76
-
NAD+
mutant H6-W187A
Pseudomonas fragi
0.8
-
D-3-hydroxybutyrate
wild-type
Pseudomonas fragi
0.88
-
D-3-hydroxybutyrate
H6-HBDH
Pseudomonas fragi
0.88
-
NAD+
mutant H6-W187T
Pseudomonas fragi
0.95
-
NAD+
mutant H6-W257A
Pseudomonas fragi
1.1
-
acetoacetate
mutant T190S
Pseudomonas fragi
1.2
-
D-3-hydroxybutyrate
mutant H6-W187Y
Pseudomonas fragi
1.3
-
acetoacetate
mutant L215V
Pseudomonas fragi
1.3
-
D-3-hydroxybutyrate
mutant H6-W187F
Pseudomonas fragi
1.5
-
NAD+
mutant L215A
Pseudomonas fragi
1.5
-
NADH
mutant T190C
Pseudomonas fragi
2.2
-
NAD+
mutant T190A
Pseudomonas fragi
3.4
-
D-3-hydroxybutyrate
mutant L215V
Pseudomonas fragi
3.7
-
D-3-hydroxybutyrate
mutant T190S
Pseudomonas fragi
7.7
-
acetoacetate
mutant T190C
Pseudomonas fragi
8.3
-
acetoacetate
mutant L215A
Pseudomonas fragi
9.2
-
D-3-hydroxybutyrate
mutant L215A
Pseudomonas fragi
25
-
D-3-hydroxybutyrate
mutant H6-H144A; mutant T190A
Pseudomonas fragi
30
-
D-3-hydroxybutyrate
mutant H6-Q94A
Pseudomonas fragi
31
-
D-3-hydroxybutyrate
mutant H6-K152R
Pseudomonas fragi
32
-
acetoacetate
mutant T190A
Pseudomonas fragi
36
-
D-3-hydroxybutyrate
mutant T190C
Pseudomonas fragi
47
-
D-3-hydroxybutyrate
mutant H6-Q196A
Pseudomonas fragi
51
-
D-3-hydroxybutyrate
mutant H6-Q196N
Pseudomonas fragi
61
-
D-3-hydroxybutyrate
mutant H6-W257A
Pseudomonas fragi
65
-
D-3-hydroxybutyrate
mutant H6-W257Y
Pseudomonas fragi
83
-
D-3-hydroxybutyrate
mutant H6-Q196E; mutant H6-W257F
Pseudomonas fragi
84
-
D-3-hydroxybutyrate
mutant H6-W187T
Pseudomonas fragi
100
-
D-3-hydroxybutyrate
mutant H6-W187A
Pseudomonas fragi
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas fragi
Q5KST5
-
-
Purification (Commentary)
Commentary
Organism
wild-type and mutants purified by metal chelating affinity chromatography followed by ion-exchange chromatography
Pseudomonas fragi
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-3-hydroxybutyrate + NAD+
-
698660
Pseudomonas fragi
acetoacetate + NADH + H+
-
-
-
r
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.5
-
acetoacetate
mutant T190A
Pseudomonas fragi
5.1
-
acetoacetate
mutant T190C
Pseudomonas fragi
6.1
-
D-3-hydroxybutyrate
mutant T190C
Pseudomonas fragi
6.7
-
D-3-hydroxybutyrate
mutant H6-W257A
Pseudomonas fragi
7.2
-
D-3-hydroxybutyrate
mutant H6-W187T
Pseudomonas fragi
12
-
D-3-hydroxybutyrate
mutant H6-W257Y
Pseudomonas fragi
21
-
D-3-hydroxybutyrate
mutant H6-H144A
Pseudomonas fragi
22
-
D-3-hydroxybutyrate
mutant H6-Q196N; mutant T190A
Pseudomonas fragi
29
-
D-3-hydroxybutyrate
mutant H6-W187A
Pseudomonas fragi
30
-
acetoacetate
mutant L215A
Pseudomonas fragi
70
-
D-3-hydroxybutyrate
mutant L215A
Pseudomonas fragi
83
-
D-3-hydroxybutyrate
mutant H6-Q196E
Pseudomonas fragi
87
-
acetoacetate
mutant L215V
Pseudomonas fragi
88
-
D-3-hydroxybutyrate
mutant H6-W257F
Pseudomonas fragi
99
-
D-3-hydroxybutyrate
mutant H6-Q196A
Pseudomonas fragi
110
-
D-3-hydroxybutyrate
mutant H6-K152R
Pseudomonas fragi
120
-
acetoacetate
wild-type
Pseudomonas fragi
125
-
acetoacetate
mutant T190S
Pseudomonas fragi
140
-
D-3-hydroxybutyrate
mutant H6-Q94A
Pseudomonas fragi
180
-
D-3-hydroxybutyrate
mutant H6-W187Y
Pseudomonas fragi
310
-
D-3-hydroxybutyrate
H6-HBDH; mutant H6-W187F
Pseudomonas fragi
370
-
D-3-hydroxybutyrate
wild-type
Pseudomonas fragi
435
-
D-3-hydroxybutyrate
mutant L215V
Pseudomonas fragi
705
-
D-3-hydroxybutyrate
mutant T190S
Pseudomonas fragi
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
-
Pseudomonas fragi
Cloned(Commentary) (protein specific)
Commentary
Organism
wild-type and mutants expressed in Escherichia coli XL1Blue harbouring pHBDH11. Wild-type HBDH and mutants containing an N-terminal His-tag expressed in Escherichia coli XL1Blue using pQE30 as a vector
Pseudomonas fragi
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystals of ternary complex of HBDH-NAD+-L-3-hydroxybutyrate and the binary complex of HBDH-NAD+. The former structure shows a closed-form conformation, which is considered an active form for catalysis, while the latter stays mostly in a open-form conformation. Crystals of mutants T190S and T190A
Pseudomonas fragi
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
H144A
catalytic efficiency (kcat/Km) is 0.2% of the activity of wild-type HBDH
Pseudomonas fragi
K152A
no activity
Pseudomonas fragi
K152E
very low activity
Pseudomonas fragi
K152Q
very low activity
Pseudomonas fragi
K152R
retains a significant level of activity
Pseudomonas fragi
L215A
both Km and kcat values are largely affected and the catalytic efficiency (kcat/Km) is less than 3% that of the wild-type enzyme
Pseudomonas fragi
L215V
Km values increase 3.5- and 4.3fold and the kcat values are 73-118% those of the wild-type toward D-3-hydroxybutyrate and acetoacetate, respectively. Mutation does not significantly change Km and kcat toward NAD+ and NADH
Pseudomonas fragi
Q196A
kcat/Km value is 0.6% that of the wild-type
Pseudomonas fragi
Q196E
substantially reduced activity
Pseudomonas fragi
Q196N
substantially reduced activity
Pseudomonas fragi
Q94A
catalytic efficiency (kcat/Km) is 1.4% of the activity of wild-type HBDH
Pseudomonas fragi
T190A
activity decreases to 0.1% that of the wild-type enzyme
Pseudomonas fragi
T190C
decreased activity
Pseudomonas fragi
T190S
retains 37% of the activity
Pseudomonas fragi
W187A
very low activity
Pseudomonas fragi
W187F
shows significant activity levels, 65% that of the wild-type enzyme
Pseudomonas fragi
W187T
shows faint activity
Pseudomonas fragi
W187Y
shows significant activity levels, 41% that of the wild-type enzyme
Pseudomonas fragi
W257A
no activity
Pseudomonas fragi
W257F
shows low activity levels, 2% that of the wild-type enzyme
Pseudomonas fragi
W257Y
shows low activity levels, 1% that of the wild-type enzyme
Pseudomonas fragi
Y155F
no activity
Pseudomonas fragi
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
L-3-hydroxybutyrate
is a competitive inhibitor
Pseudomonas fragi
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
NADH
wild-type
Pseudomonas fragi
0.02
-
NADH
mutant T190S
Pseudomonas fragi
0.03
-
NADH
mutant L215V
Pseudomonas fragi
0.1
-
NADH
mutant T190A
Pseudomonas fragi
0.12
-
NAD+
mutant H6-K152R; mutant H6-Q196A; mutant H6-Q196E
Pseudomonas fragi
0.17
-
NAD+
H6-HBDH
Pseudomonas fragi
0.19
-
NAD+
mutant H6-Q94A
Pseudomonas fragi
0.2
-
NAD+
mutant H6-Q196N
Pseudomonas fragi
0.21
-
NAD+
mutant H6-W187Y
Pseudomonas fragi
0.24
-
NAD+
mutant H6-W187F; wild-type
Pseudomonas fragi
0.29
-
NAD+
mutant L215V
Pseudomonas fragi
0.35
-
NAD+
mutant H6-H144A
Pseudomonas fragi
0.37
-
acetoacetate
wild-type
Pseudomonas fragi
0.49
-
NAD+
mutant H6-W257F
Pseudomonas fragi
0.5
-
NADH
mutant L215A
Pseudomonas fragi
0.69
-
NAD+
mutant T190C
Pseudomonas fragi
0.71
-
NAD+
mutant T190S
Pseudomonas fragi
0.74
-
NAD+
mutant H6-W257Y
Pseudomonas fragi
0.76
-
NAD+
mutant H6-W187A
Pseudomonas fragi
0.8
-
D-3-hydroxybutyrate
wild-type
Pseudomonas fragi
0.88
-
D-3-hydroxybutyrate
H6-HBDH
Pseudomonas fragi
0.88
-
NAD+
mutant H6-W187T
Pseudomonas fragi
0.95
-
NAD+
mutant H6-W257A
Pseudomonas fragi
1.1
-
acetoacetate
mutant T190S
Pseudomonas fragi
1.2
-
D-3-hydroxybutyrate
mutant H6-W187Y
Pseudomonas fragi
1.3
-
acetoacetate
mutant L215V
Pseudomonas fragi
1.3
-
D-3-hydroxybutyrate
mutant H6-W187F
Pseudomonas fragi
1.5
-
NAD+
mutant L215A
Pseudomonas fragi
1.5
-
NADH
mutant T190C
Pseudomonas fragi
2.2
-
NAD+
mutant T190A
Pseudomonas fragi
3.4
-
D-3-hydroxybutyrate
mutant L215V
Pseudomonas fragi
3.7
-
D-3-hydroxybutyrate
mutant T190S
Pseudomonas fragi
7.7
-
acetoacetate
mutant T190C
Pseudomonas fragi
8.3
-
acetoacetate
mutant L215A
Pseudomonas fragi
9.2
-
D-3-hydroxybutyrate
mutant L215A
Pseudomonas fragi
25
-
D-3-hydroxybutyrate
mutant H6-H144A; mutant T190A
Pseudomonas fragi
30
-
D-3-hydroxybutyrate
mutant H6-Q94A
Pseudomonas fragi
31
-
D-3-hydroxybutyrate
mutant H6-K152R
Pseudomonas fragi
32
-
acetoacetate
mutant T190A
Pseudomonas fragi
36
-
D-3-hydroxybutyrate
mutant T190C
Pseudomonas fragi
47
-
D-3-hydroxybutyrate
mutant H6-Q196A
Pseudomonas fragi
51
-
D-3-hydroxybutyrate
mutant H6-Q196N
Pseudomonas fragi
61
-
D-3-hydroxybutyrate
mutant H6-W257A
Pseudomonas fragi
65
-
D-3-hydroxybutyrate
mutant H6-W257Y
Pseudomonas fragi
83
-
D-3-hydroxybutyrate
mutant H6-Q196E; mutant H6-W257F
Pseudomonas fragi
84
-
D-3-hydroxybutyrate
mutant H6-W187T
Pseudomonas fragi
100
-
D-3-hydroxybutyrate
mutant H6-W187A
Pseudomonas fragi
Purification (Commentary) (protein specific)
Commentary
Organism
wild-type and mutants purified by metal chelating affinity chromatography followed by ion-exchange chromatography
Pseudomonas fragi
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-3-hydroxybutyrate + NAD+
-
698660
Pseudomonas fragi
acetoacetate + NADH + H+
-
-
-
r
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.5
-
acetoacetate
mutant T190A
Pseudomonas fragi
5.1
-
acetoacetate
mutant T190C
Pseudomonas fragi
6.1
-
D-3-hydroxybutyrate
mutant T190C
Pseudomonas fragi
6.7
-
D-3-hydroxybutyrate
mutant H6-W257A
Pseudomonas fragi
7.2
-
D-3-hydroxybutyrate
mutant H6-W187T
Pseudomonas fragi
12
-
D-3-hydroxybutyrate
mutant H6-W257Y
Pseudomonas fragi
21
-
D-3-hydroxybutyrate
mutant H6-H144A
Pseudomonas fragi
22
-
D-3-hydroxybutyrate
mutant H6-Q196N; mutant T190A
Pseudomonas fragi
29
-
D-3-hydroxybutyrate
mutant H6-W187A
Pseudomonas fragi
30
-
acetoacetate
mutant L215A
Pseudomonas fragi
70
-
D-3-hydroxybutyrate
mutant L215A
Pseudomonas fragi
83
-
D-3-hydroxybutyrate
mutant H6-Q196E
Pseudomonas fragi
87
-
acetoacetate
mutant L215V
Pseudomonas fragi
88
-
D-3-hydroxybutyrate
mutant H6-W257F
Pseudomonas fragi
99
-
D-3-hydroxybutyrate
mutant H6-Q196A
Pseudomonas fragi
110
-
D-3-hydroxybutyrate
mutant H6-K152R
Pseudomonas fragi
120
-
acetoacetate
wild-type
Pseudomonas fragi
125
-
acetoacetate
mutant T190S
Pseudomonas fragi
140
-
D-3-hydroxybutyrate
mutant H6-Q94A
Pseudomonas fragi
180
-
D-3-hydroxybutyrate
mutant H6-W187Y
Pseudomonas fragi
310
-
D-3-hydroxybutyrate
H6-HBDH; mutant H6-W187F
Pseudomonas fragi
370
-
D-3-hydroxybutyrate
wild-type
Pseudomonas fragi
435
-
D-3-hydroxybutyrate
mutant L215V
Pseudomonas fragi
705
-
D-3-hydroxybutyrate
mutant T190S
Pseudomonas fragi
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
-
Pseudomonas fragi
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
-
-
-
1
-
-
2
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
2
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
737914
Yeon
-
Structural basis for the subst ...
Alcaligenes faecalis
Biotechnol. Bioprocess Eng.
21
364-372
2016
-
-
1
-
15
-
-
15
-
-
-
1
-
1
-
-
1
-
-
-
-
-
2
-
-
-
-
15
-
-
-
1
-
-
-
-
-
1
1
-
15
-
-
-
-
15
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
15
-
-
-
-
-
-
-
-
13
13
739558
Davuluri
Inactivation of 3-hydroxybutyr ...
Danio rerio
Proc. Natl. Acad. Sci. USA
113
E1460-E1469
2016
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
737467
Scaturro
Identification and characteriz ...
Legionella pneumophila subsp. pneumophila, Legionella pneumophila subsp. pneumophila DSM 7513
APMIS
123
330-341
2015
-
-
-
-
-
-
-
-
1
-
-
2
-
6
-
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3-Hydroxybutyrate oligomer hyd ...
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Mountassif
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695653
Takanashi
Characterization of a novel 3- ...
Ralstonia pickettii, Ralstonia pickettii T1
Antonie van Leeuwenhoek
95
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Closed complex of the D-3-hydr ...
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684149
Hoque
The structures of Alcaligenes ...
Alcaligenes faecalis
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689351
Mountassif
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Biochemical and histological a ...
Jaculus orientalis
Pestic. Biochem. Physiol.
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679792
Paithankar
Cosubstrate-induced dynamics o ...
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Uchino
Isolated poly(3-hydroxybutyrat ...
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2007
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685409
Mountassif
Prehibernation and hibernation ...
Jaculus orientalis
Biochimie
89
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668251
Feller
Molecular basis of substrate r ...
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ChemBioChem
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668322
Mountassif
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Characterization of two D-b-hy ...
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Comp. Biochem. Physiol. B
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2006
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Guo
Characterization of human DHRS ...
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Takanashi
Characterization of two 3-hydr ...
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Ito
D-3-hydroxybutyrate dehydrogen ...
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5
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667070
Nakajima
Crystallization and preliminar ...
Pseudomonas fragi
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656326
Takanashi
Biochemical and genetic charac ...
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1
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2
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1
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1
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655126
Kabine
Hibernation impact on the cata ...
Jaculus orientalis
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9
2
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3
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3
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1
1
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1
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655261
Nasser
Purification and characterizat ...
Camelus dromedarius
Comp. Biochem. Physiol. B
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2002
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3
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3
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2
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3
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2
1
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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
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2000
1
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1
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286513
Green
Wild type and mutant human hea ...
Bos taurus, Homo sapiens
Biochemistry
35
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1996
2
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4
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7
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286514
Klein
Specific interaction of(R)-3-h ...
Bos taurus
Biochemistry
35
3044-3049
1996
1
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286515
Szewczyk
Occurence, purification and pr ...
Staphylococcus xylosus
Acta Microbiol. Pol.
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286516
Adam
Monoclonal antibodies for stru ...
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Biochem. J.
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1993
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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
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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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1993
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286519
Marks
Molecular cloning and characte ...
Homo sapiens
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1
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3
-
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1
1
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286520
Bailly
Post-transcriptional analysis ...
Rattus norvegicus
Biol. Cell.
73
121-129
1991
1
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-
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1
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1
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2
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4
3
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1
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-
-
286521
McIntyre
Comparison of 3-hydroxybutyrat ...
Bos taurus, Rattus norvegicus
Arch. Biochem. Biophys.
262
85-98
1988
2
-
-
-
-
-
-
4
4
-
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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7
2
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2
2
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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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-
-
-
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-
-
-
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286523
Worral
3-Hydroxyisobutyrate dehydroge ...
Rhodobacter sphaeroides
Biochem. J.
241
297-300
1987
1
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1
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4
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1
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1
-
1
-
-
-
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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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1
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1
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1
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7
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1
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1
-
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-
-
-
2
-
-
-
-
-
-
-
-
-
286525
Dubois
Cyanylation of 3-hydroxybutyra ...
Bos taurus
Biol. Chem. Hoppe-Seyler
367
343-353
1986
1
-
-
-
-
-
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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8
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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-
-
-
286526
Matyskova I.; Kovar
-
Purification and properties of ...
Paracoccus denitrificans
Biochim. Biophys. Acta
839
300-307
1985
1
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2
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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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
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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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-
-
-
-
-
-
-
-
-
-
-
-
-
286529
MacGill
-
D-3-Hydroxybutyrate dehydrogen ...
Rattus norvegicus
Biochem. Soc. Trans.
607
788
1984
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
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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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-
-
-
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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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-
-
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1
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2
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
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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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286531
Scawen
The rapid purification of 3-hy ...
Rhodobacter sphaeroides
Biochem. J.
203
699-705
1982
1
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-
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2
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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1
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1
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1
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1
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1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286528
Phelps
Inhibition of D(-)-beta-hydrox ...
Bos taurus
Biochemistry
20
459-463
1981
1
-
-
-
-
-
4
1
1
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-
1
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2
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-
1
1
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2
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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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4
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1
1
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1
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1
1
-
2
-
-
-
-
-
-
-
-
-
-
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-
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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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-
-
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8
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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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8
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1
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1
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-
-
-
-
-
-
-
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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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-
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1
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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
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1
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1
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1
2
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1
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-
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-
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-
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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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17
4
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2
2
1
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2
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1
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1
1
1
1
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-
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1
1
-
1
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-
6
-
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1
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-
-
-
17
-
4
-
2
2
1
-
-
-
1
-
-
1
1
1
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
286535
Phelps
Inhibition of D(-)-beta-hydrox ...
Bos taurus
Biochemistry
20
453-458
1981
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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-
1
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-
-
-
-
-
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1
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1
-
-
1
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6
-
4
1
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
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-
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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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-
-
-
-
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8
1
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1
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3
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-
4
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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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-
-
-
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-
8
1
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1
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-
-
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-
4
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1
-
-
-
-
-
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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
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1
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3
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1
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1
-
-
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1
-
-
1
-
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-
-
10
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
286538
McIntyre
The orientation of D-beta-hydr ...
Bos taurus
Biochim. Biophys. Acta
513
255-267
1978
1
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2
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2
1
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1
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-
-
-
-
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-
1
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-
1
-
-
1
-
-
-
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-
-
-
2
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-
1
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-
-
-
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2
1
-
1
-
-
-
-
-
-
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-
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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
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2
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1
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-
1
-
1
-
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-
1
-
2
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
-
2
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1
-
-
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1
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1
-
1
-
-
-
1
-
2
1
-
-
-
-
-
-
-
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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
-
-
-
-
3
-
3
-
-
-
-
-
3
-
-
3
-
-
-
-
-
-
-
-
3
-
-
-
3
-
-
3
-
-
-
-
20
-
-
-
-
-
3
-
-
-
-
-
3
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286541
Thompson
Characterization and partial p ...
Bacillus cereus, Bacillus cereus T
Can. J. Microbiol.
19
673-677
1973
1
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-
-
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2
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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
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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-
-
-
-
-
2
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1
-
2
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1
-
-
1
1
2
-
-
-
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1
1
-
-
-
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-
-
-
-
286542
Nielsen
Mitochondrial D-beta-hydroxybu ...
Bos taurus
J. Biol. Chem.
248
2549-2555
1973
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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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
-
1
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-
-
-
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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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5
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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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5
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-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
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