Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.5.12 extracted from

  • Peersen, O.; Pratt, E.; Truong, H.; Ho, C.; Rule, G.
    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 (1990), Biochemistry, 29, 3256-3262.
    View publication on PubMed
Search for more literature for 1.1.5.12

Crystallization (Commentary)

Crystallization (Comment) 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

Protein Variants

Protein Variants Comment 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 Comment 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 Escherichia coli
0.9
-
 (R)-lactate 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 Escherichia coli
1.5
-
 (R)-lactate 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 UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-lactate + a quinone
-
 Escherichia coli pyruvate + a quinol
-
 ?