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show all sequences of 1.1.5.12

Site-specific incorporation of 5-fluorotryptophan as a probe of the structure and function of the membrane-bound D-lactate dehydrogenase of Escherichia coli: A19F nuclear magnetic resonance study

Peersen, O.; Pratt, E.; Truong, H.; Ho, C.; Rule, G.; Biochemistry 29, 3256-3262 (1990)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
fluorine-19 nuclear magnetic resonance spectroscopy of 5-fluorotryptophan-labeled enzyme. The membrane-bound D-lactate dehydrogenase may have the two-domain structure of many cytoplasmic dehydrogenases but with the addition of a membrane-binding domain between the catalytic and cofactor-binding domains
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
F12W
increase in activtiy
Escherichia coli
F176W
about 25% of wild-type vmax
Escherichia coli
F263W
loss of activity
Escherichia coli
F279W
loss of activity
Escherichia coli
F326W
loss of activity
Escherichia coli
F340W
about 35% of wild-type vmax
Escherichia coli
F361W
activity similar to wild-type
Escherichia coli
F39W
about 50% of wild-type vmax
Escherichia coli
F412W
loss of activity
Escherichia coli
F435W
about 25% of wild-type vmax
Escherichia coli
F490W
loss of activity
Escherichia coli
F544W
loss of activity
Escherichia coli
I152W
loss of activity
Escherichia coli
I193W
loss of activity
Escherichia coli
I99W
loss of activity
Escherichia coli
L110W
loss of activity
Escherichia coli
L203W
loss of activity
Escherichia coli
L456W
loss of activity
Escherichia coli
L517W
about 50% of wild-type vmax
Escherichia coli
Y243W
activity similar to wild-type
Escherichia coli
Y309W
loss of activity
Escherichia coli
Y388W
about 75% of wild-type vmax
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.6
-
(R)-lactate
mutant F39W, pH 7.2, 20°C
Escherichia coli
0.9
-
(R)-lactate
mutant F176W, pH 7.2, 20°C; mutant F340W, pH 7.2, 20°C
Escherichia coli
1.1
-
(R)-lactate
mutant F435W, pH 7.2, 20°C
Escherichia coli
1.5
-
(R)-lactate
mutant Y243W, pH 7.2, 20°C; mutant Y388W, pH 7.2, 20°C
Escherichia coli
1.6
-
(R)-lactate
wild-type, pH 7.2, 20°C
Escherichia coli
1.8
-
(R)-lactate
mutant L517W, pH 7.2, 20°C
Escherichia coli
2.1
-
(R)-lactate
mutant F12W, pH 7.2, 20°C
Escherichia coli
2.3
-
(R)-lactate
mutant F361W, pH 7.2, 20°C
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-lactate + a quinone
-
740031
Escherichia coli
pyruvate + a quinol
-
-
-
?
Crystallization (Commentary) (protein specific)
Crystallization
Organism
fluorine-19 nuclear magnetic resonance spectroscopy of 5-fluorotryptophan-labeled enzyme. The membrane-bound D-lactate dehydrogenase may have the two-domain structure of many cytoplasmic dehydrogenases but with the addition of a membrane-binding domain between the catalytic and cofactor-binding domains
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
F12W
increase in activtiy
Escherichia coli
F176W
about 25% of wild-type vmax
Escherichia coli
F263W
loss of activity
Escherichia coli
F279W
loss of activity
Escherichia coli
F326W
loss of activity
Escherichia coli
F340W
about 35% of wild-type vmax
Escherichia coli
F361W
activity similar to wild-type
Escherichia coli
F39W
about 50% of wild-type vmax
Escherichia coli
F412W
loss of activity
Escherichia coli
F435W
about 25% of wild-type vmax
Escherichia coli
F490W
loss of activity
Escherichia coli
F544W
loss of activity
Escherichia coli
I152W
loss of activity
Escherichia coli
I193W
loss of activity
Escherichia coli
I99W
loss of activity
Escherichia coli
L110W
loss of activity
Escherichia coli
L203W
loss of activity
Escherichia coli
L456W
loss of activity
Escherichia coli
L517W
about 50% of wild-type vmax
Escherichia coli
Y243W
activity similar to wild-type
Escherichia coli
Y309W
loss of activity
Escherichia coli
Y388W
about 75% of wild-type vmax
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.6
-
(R)-lactate
mutant F39W, pH 7.2, 20°C
Escherichia coli
0.9
-
(R)-lactate
mutant F176W, pH 7.2, 20°C; mutant F340W, pH 7.2, 20°C
Escherichia coli
1.1
-
(R)-lactate
mutant F435W, pH 7.2, 20°C
Escherichia coli
1.5
-
(R)-lactate
mutant Y243W, pH 7.2, 20°C; mutant Y388W, pH 7.2, 20°C
Escherichia coli
1.6
-
(R)-lactate
wild-type, pH 7.2, 20°C
Escherichia coli
1.8
-
(R)-lactate
mutant L517W, pH 7.2, 20°C
Escherichia coli
2.1
-
(R)-lactate
mutant F12W, pH 7.2, 20°C
Escherichia coli
2.3
-
(R)-lactate
mutant F361W, pH 7.2, 20°C
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-lactate + a quinone
-
740031
Escherichia coli
pyruvate + a quinol
-
-
-
?
Other publictions for EC 1.1.5.12
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)
727253
Kato
Quinone-dependent D-lactate de ...
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032
BMC Microbiol.
10
321
2010
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1
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25
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8
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1
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1
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8
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1
1
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740031
Peersen
Site-specific incorporation of ...
Escherichia coli
Biochemistry
29
3256-3262
1990
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1
22
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8
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1
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1
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1
22
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8
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1
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740030
Matsushita
D-Lactate oxidation and genera ...
Escherichia coli, Escherichia coli GR19N
Biochemistry
25
2321-2327
1986
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3
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1
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4
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1
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4
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1
1
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740029
Pratt
Membrane-bound D-lactate dehyd ...
Escherichia coli, Escherichia coli W3110trpA33
Biochemistry
18
312-316
1979
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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2
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
1
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1
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1
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1
2
2
1
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1
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740028
Futai
Membrane D-lactate dehydrogena ...
Escherichia coli
Biochemistry
12
2468-2474
1973
1
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1
4
1
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2
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1
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1
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2
3
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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4
1
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2
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1
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2
3
1
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1
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740643
Kohn
Mechanisms of active transport ...
Escherichia coli, Escherichia coli ML 308-225
J. Biol. Chem.
248
7012-7017
1973
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2
4
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1
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3
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1
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8
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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4
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1
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1
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8
1
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2
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