BRENDA - Enzyme Database

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)
EC Number
Crystallization
Organism
1.1.5.12
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
EC Number
Amino acid exchange
Commentary
Organism
1.1.5.12
F12W
increase in activtiy
Escherichia coli
1.1.5.12
F176W
about 25% of wild-type vmax
Escherichia coli
1.1.5.12
F263W
loss of activity
Escherichia coli
1.1.5.12
F279W
loss of activity
Escherichia coli
1.1.5.12
F326W
loss of activity
Escherichia coli
1.1.5.12
F340W
about 35% of wild-type vmax
Escherichia coli
1.1.5.12
F361W
activity similar to wild-type
Escherichia coli
1.1.5.12
F39W
about 50% of wild-type vmax
Escherichia coli
1.1.5.12
F412W
loss of activity
Escherichia coli
1.1.5.12
F435W
about 25% of wild-type vmax
Escherichia coli
1.1.5.12
F490W
loss of activity
Escherichia coli
1.1.5.12
F544W
loss of activity
Escherichia coli
1.1.5.12
I152W
loss of activity
Escherichia coli
1.1.5.12
I193W
loss of activity
Escherichia coli
1.1.5.12
I99W
loss of activity
Escherichia coli
1.1.5.12
L110W
loss of activity
Escherichia coli
1.1.5.12
L203W
loss of activity
Escherichia coli
1.1.5.12
L456W
loss of activity
Escherichia coli
1.1.5.12
L517W
about 50% of wild-type vmax
Escherichia coli
1.1.5.12
Y243W
activity similar to wild-type
Escherichia coli
1.1.5.12
Y309W
loss of activity
Escherichia coli
1.1.5.12
Y388W
about 75% of wild-type vmax
Escherichia coli
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.1.5.12
0.6
-
(R)-lactate
mutant F39W, pH 7.2, 20C
Escherichia coli
1.1.5.12
0.9
-
(R)-lactate
mutant F176W, pH 7.2, 20C; mutant F340W, pH 7.2, 20C
Escherichia coli
1.1.5.12
1.1
-
(R)-lactate
mutant F435W, pH 7.2, 20C
Escherichia coli
1.1.5.12
1.5
-
(R)-lactate
mutant Y243W, pH 7.2, 20C; mutant Y388W, pH 7.2, 20C
Escherichia coli
1.1.5.12
1.6
-
(R)-lactate
wild-type, pH 7.2, 20C
Escherichia coli
1.1.5.12
1.8
-
(R)-lactate
mutant L517W, pH 7.2, 20C
Escherichia coli
1.1.5.12
2.1
-
(R)-lactate
mutant F12W, pH 7.2, 20C
Escherichia coli
1.1.5.12
2.3
-
(R)-lactate
mutant F361W, pH 7.2, 20C
Escherichia coli
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.1.5.12
Escherichia coli
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.1.5.12
(R)-lactate + a quinone
-
740031
Escherichia coli
pyruvate + a quinol
-
-
-
?
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.1.5.12
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)
EC Number
Amino acid exchange
Commentary
Organism
1.1.5.12
F12W
increase in activtiy
Escherichia coli
1.1.5.12
F176W
about 25% of wild-type vmax
Escherichia coli
1.1.5.12
F263W
loss of activity
Escherichia coli
1.1.5.12
F279W
loss of activity
Escherichia coli
1.1.5.12
F326W
loss of activity
Escherichia coli
1.1.5.12
F340W
about 35% of wild-type vmax
Escherichia coli
1.1.5.12
F361W
activity similar to wild-type
Escherichia coli
1.1.5.12
F39W
about 50% of wild-type vmax
Escherichia coli
1.1.5.12
F412W
loss of activity
Escherichia coli
1.1.5.12
F435W
about 25% of wild-type vmax
Escherichia coli
1.1.5.12
F490W
loss of activity
Escherichia coli
1.1.5.12
F544W
loss of activity
Escherichia coli
1.1.5.12
I152W
loss of activity
Escherichia coli
1.1.5.12
I193W
loss of activity
Escherichia coli
1.1.5.12
I99W
loss of activity
Escherichia coli
1.1.5.12
L110W
loss of activity
Escherichia coli
1.1.5.12
L203W
loss of activity
Escherichia coli
1.1.5.12
L456W
loss of activity
Escherichia coli
1.1.5.12
L517W
about 50% of wild-type vmax
Escherichia coli
1.1.5.12
Y243W
activity similar to wild-type
Escherichia coli
1.1.5.12
Y309W
loss of activity
Escherichia coli
1.1.5.12
Y388W
about 75% of wild-type vmax
Escherichia coli
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.1.5.12
0.6
-
(R)-lactate
mutant F39W, pH 7.2, 20C
Escherichia coli
1.1.5.12
0.9
-
(R)-lactate
mutant F176W, pH 7.2, 20C; mutant F340W, pH 7.2, 20C
Escherichia coli
1.1.5.12
1.1
-
(R)-lactate
mutant F435W, pH 7.2, 20C
Escherichia coli
1.1.5.12
1.5
-
(R)-lactate
mutant Y243W, pH 7.2, 20C; mutant Y388W, pH 7.2, 20C
Escherichia coli
1.1.5.12
1.6
-
(R)-lactate
wild-type, pH 7.2, 20C
Escherichia coli
1.1.5.12
1.8
-
(R)-lactate
mutant L517W, pH 7.2, 20C
Escherichia coli
1.1.5.12
2.1
-
(R)-lactate
mutant F12W, pH 7.2, 20C
Escherichia coli
1.1.5.12
2.3
-
(R)-lactate
mutant F361W, pH 7.2, 20C
Escherichia coli
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.1.5.12
(R)-lactate + a quinone
-
740031
Escherichia coli
pyruvate + a quinol
-
-
-
?