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Literature summary extracted from

  • Shinagawa, E.; Matsushita, K.; Adachi, O.; Ameyama, M.
    Purification and characterization of D-sorbitol dehydrogenase from membrane of Gluconobacter suboxydans var. alpha (1982), Agric. Biol. Chem., 46, 135-141.
No PubMed abstract available

General Stability

EC Number General Stability Organism
1.1.99.21 D-sorbitol stabilizes during solubilization and purification Gluconobacter oxydans
1.1.99.21 ionic detergents, such as cetylpyridinium chloride, cetyltrimethyl ammonium bromide and sodium stearate, inactivate Gluconobacter oxydans
1.1.99.21 Triton X-100, best detergent for solubilization Gluconobacter oxydans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.99.21 30
-
D-sorbitol
-
Gluconobacter oxydans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.99.21 cytoplasmic membrane
-
Gluconobacter oxydans
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.99.21 KCl activation Gluconobacter oxydans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.99.21 17000
-
1 * 63000 + 1 * 51000 + 1 * 17000, dissociation into 3 components, a flavoprotein (MW 63000), a cytochrome c (MW 51000) and an unknown polypeptide (MW 17000), SDS-PAGE Gluconobacter oxydans
1.1.99.21 51000
-
1 * 63000 + 1 * 51000 + 1 * 17000, dissociation into 3 components, a flavoprotein (MW 63000), a cytochrome c (MW 51000) and an unknown polypeptide (MW 17000), SDS-PAGE Gluconobacter oxydans
1.1.99.21 63000
-
1 * 63000 + 1 * 51000 + 1 * 17000, dissociation into 3 components, a flavoprotein (MW 63000), a cytochrome c (MW 51000) and an unknown polypeptide (MW 17000), SDS-PAGE Gluconobacter oxydans
1.1.99.21 131000
-
calculated sum of each MW of the 3 subunits Gluconobacter oxydans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.99.21 D-sorbitol + acceptor Gluconobacter oxydans high specificity L-sorbose + reduced acceptor
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.99.21 Gluconobacter oxydans
-
var. alpha IFO 3254
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.99.21
-
Gluconobacter oxydans

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.99.21 433
-
-
Gluconobacter oxydans

Storage Stability

EC Number Storage Stability Organism
1.1.99.21 5°C, 50% loss of activity overnight Gluconobacter oxydans
1.1.99.21 5°C, storage for several months leads to cytochrome c decomposition Gluconobacter oxydans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.99.21 D-mannitol + acceptor oxidation at 5% the rate of D-sorbitol Gluconobacter oxydans ? + reduced acceptor
-
?
1.1.99.21 D-sorbitol + acceptor high specificity Gluconobacter oxydans L-sorbose + reduced acceptor
-
?
1.1.99.21 D-sorbitol + acceptor high specificity, the following dyes act in vitro as acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, potassium ferricyanide, nitro blue tetrazolium or tetramethyl-p-phenylenediamine Gluconobacter oxydans L-sorbose + reduced acceptor
-
?
1.1.99.21 additional information no oxidation of D-arabitol, L-iditol, meso-erythritol, galactitol, dulcitol, ribitol, xylitol Gluconobacter oxydans ?
-
?

Subunits

EC Number Subunits Comment Organism
1.1.99.21 More 1 * 63000 + 1 * 51000 + 1 * 17000, dissociation into 3 components, a flavoprotein (MW 63000), a cytochrome c (MW 51000) and an unknown polypeptide (MW 17000), SDS-PAGE Gluconobacter oxydans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.99.21 25
-
-
Gluconobacter oxydans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.99.21 4.5
-
-
Gluconobacter oxydans

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.99.21 cytochrome c tightly bound , dehydrogenase-cytochrome c complex, separable by SDS-PAGE Gluconobacter oxydans
1.1.99.21 FAD flavoprotein, covalently bound, 0.4 mol/mol enzyme Gluconobacter oxydans
1.1.99.21 additional information NAD+, NADP+ or molecular oxygen are completely inactive Gluconobacter oxydans