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Literature summary 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

Crystallization (Commentary)

EC Number Crystallization (Comment) 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

Protein Variants

EC Number Protein Variants Comment 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 Comment Organism Structure
1.1.5.12 0.6
-
(R)-lactate mutant F39W, pH 7.2, 20°C Escherichia coli
1.1.5.12 0.9
-
(R)-lactate mutant F176W, pH 7.2, 20°C Escherichia coli
1.1.5.12 0.9
-
(R)-lactate mutant F340W, pH 7.2, 20°C Escherichia coli
1.1.5.12 1.1
-
(R)-lactate mutant F435W, pH 7.2, 20°C Escherichia coli
1.1.5.12 1.5
-
(R)-lactate mutant Y243W, pH 7.2, 20°C Escherichia coli
1.1.5.12 1.5
-
(R)-lactate mutant Y388W, pH 7.2, 20°C Escherichia coli
1.1.5.12 1.6
-
(R)-lactate wild-type, pH 7.2, 20°C Escherichia coli
1.1.5.12 1.8
-
(R)-lactate mutant L517W, pH 7.2, 20°C Escherichia coli
1.1.5.12 2.1
-
(R)-lactate mutant F12W, pH 7.2, 20°C Escherichia coli
1.1.5.12 2.3
-
(R)-lactate mutant F361W, pH 7.2, 20°C Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.12 Escherichia coli
-
-
-

Substrates and Products (Substrate)

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