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Literature summary for 1.1.99.21 extracted from

  • Yang, X.P.; Wei, L.J.; Ye, J.B.; Yin, B.; Wei, D.Z.
    A pyrroloquinoline quinine-dependent membrane-bound d-sorbitol dehydrogenase from Gluconobacter oxydans exhibits an ordered Bi Bi reaction mechanism (2008), Arch. Biochem. Biophys., 477, 206-210.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
D-sorbose non-competitive inhibition, sorbitol or phenazine methosulfate as substrates Gluconobacter oxydans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0257
-
 ubiquinone-2
-
 Gluconobacter oxydans
0.0314
-
 phenazine methosulfate
-
 Gluconobacter oxydans
16.8
-
 D-sorbitol ubiquinone-2 as electron acceptor Gluconobacter oxydans
23.2
-
 D-sorbitol phenazine methosulfate as electron acceptor Gluconobacter oxydans

Organism

Organism UniProt Comment Textmining
Gluconobacter oxydans
-
 IFO 3255
-

Purification (Commentary)

Purification (Comment) Organism
by CM-cellulose and sephacryl HR 400 column chromatography Gluconobacter oxydans

Storage Stability

Storage Stability Organism
stable at 80°C for more than two months in the presence of 0.1% Tween-20 Gluconobacter oxydans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-sorbitol + phenazine methosulfate the catalytic reaction follows an ordered Bi Bi mechanism, the native mSLDH bears two different substrate-binding sites, one for ubiquinone using as electron acceptor and the other for D-sorbitol, in addition to PQQ-binding and Mg2+-binding sites in the catalytic center Gluconobacter oxydans ?
-
 ?
D-sorbitol + ubiquinone-2
-
 Gluconobacter oxydans ?
-
 ?

Synonyms

Synonyms Comment Organism
D-sorbitol dehydrogenase membrane-bound pyrroloquinoline quinine dependent, mSLDH Gluconobacter oxydans

Cofactor

Cofactor Comment Organism Structure
additional information pyrroloquinoline quinine Gluconobacter oxydans