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Literature summary for 1.1.1.271 extracted from

  • Rosano, C.; Bisso, A.; Izzo, G.; Tonetti, M.; Sturla, L.; De Flora, A.; Bolognesi, M.
    Probing the catalytic mechanism of GDP-4-keto-6-deoxy-D-mannose epimerase/reductase by kinetic and crystallographic characterization of site-specific mutants (2000), J. Mol. Biol., 303, 77-91.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
C109A lower Km than wild-type enzyme Escherichia coli
H179N lower Km than wild-type enzyme Escherichia coli
K140R higher Km than wild-type enzyme Escherichia coli
K140S higher Km than wild-type enzyme Escherichia coli
R187A lower Km than wild-type enzyme Escherichia coli
S107A lower Km than wild-type enzyme Escherichia coli
Y136E no enzymatic activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Km values for various mutants Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000 36000 SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
homogeneity Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4
-
wild type enzyme is stable for several weeks in phosphate buffered saline at concentrations higher than 10 mg/ml, stability of mutants differ from wild type enzyme Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information values for various mutants Escherichia coli