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Literature summary for 1.1.1.175 extracted from

  • Bonete, M.J.; Pire, C.; Llorca, F.I.; Camacho, M.L.
    Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: Enzyme purification, characterization and N-terminal sequence (1996), FEBS Lett., 383, 227-229.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
EDTA 2 mM Haloferax mediterranei

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53000
-
2 * 53000, SDS-PAGE Haloferax mediterranei
89000
-
gel filtration Haloferax mediterranei

Organism

Organism UniProt Comment Textmining
Haloferax mediterranei Q977U7
-
-
Haloferax mediterranei DSM 1411 Q977U7
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Haloferax mediterranei

Storage Stability

Storage Stability Organism
4°C, stable for several months Haloferax mediterranei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-xylose + NAD+ 79% of the activity with D-glucose and NADP+. The enzyme shows also activity with D-xylose and NAD+ as cofactor, D-glucose (NADP+ or NAD+ as cofactor), D-fucose (cofactor NADP+) and D-galactose (cofactor NADP+) Haloferax mediterranei ?
-
?
D-xylose + NAD+ 79% of the activity with D-glucose and NADP+. The enzyme shows also activity with D-xylose and NAD+ as cofactor, D-glucose (NADP+ or NAD+ as cofactor), D-fucose (cofactor NADP+) and D-galactose (cofactor NADP+) Haloferax mediterranei DSM 1411 ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 53000, SDS-PAGE Haloferax mediterranei

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
half-life: 56.8 h, in the presence of 3 M NaCl, stability decreases significantly with lower salt concentrations Haloferax mediterranei