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Literature summary for 1.1.5.5 extracted from

  • Chen, Z.; Baruch, P.; Mathews, F.S.; Matsushita, K.; Yamashita, T.; Toyama, H.; Adachi, O.
    Crystallization and preliminary diffraction studies of two quinoprotein alcohol dehydrogenases (ADHs): a soluble monomeric ADH from Pseudomonas putida HK5 (ADH-IIB) and a heterotrimeric membrane-bound ADH from Gluconobacter suboxydans (ADH-GS). (1999), Acta Crystallogr. Sect. D, 55, 1933-1936.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
ADH-GS, 10 mg/ml protein in 100 mM sodium acetate buffer, pH 4.5, 0.34 mM n-dodecyl-beta-D-maltoside or 0.16 mM C12E8 and either 150 mM ammonium sulfate/6% PEG 3350 or 1.3 M ammonium sulfate only, with or without 2 mM Ca2+, X-ray diffraction structure determination and analysis at 3.0-5.0 A resolution, heavy atom labeling Gluconobacter oxydans

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane associated, ADH-GS Gluconobacter oxydans 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+
-
Gluconobacter oxydans

Organism

Organism UniProt Comment Textmining
Gluconobacter oxydans
-
-
-

Subunits

Subunits Comment Organism
trimer heterotrimer with unequal numers of heme groups, overview Gluconobacter oxydans

Synonyms

Synonyms Comment Organism
ADH-GS
-
Gluconobacter oxydans
ADH-IIB
-
-
More the enzyme is a type III ADH Gluconobacter oxydans
quinocytochrome alcohol dehydrogenase GS
-
Gluconobacter oxydans
quinocytochrome alcohol dehydrogenase IIB
-
-

Cofactor

Cofactor Comment Organism Structure
cytochrome
-
Gluconobacter oxydans
heme 4 molecules per enzyme molecule Gluconobacter oxydans
pyrroloquinoline quinone dependent on, 1 molecule per enzyme molecule Gluconobacter oxydans