Inhibitors | Comment | Organism | Structure |
---|---|---|---|
D-sorbose | non-competitive inhibition, sorbitol or phenazine methosulfate as substrates | Gluconobacter oxydans |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Gluconobacter oxydans | - |
IFO 3255 | - |
Purification (Comment) | Organism |
---|---|
by CM-cellulose and sephacryl HR 400 column chromatography | Gluconobacter oxydans |
Storage Stability | Organism |
---|---|
stable at 80°C for more than two months in the presence of 0.1% Tween-20 | Gluconobacter oxydans |
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 | Comment | Organism |
---|---|---|
D-sorbitol dehydrogenase | membrane-bound pyrroloquinoline quinine dependent, mSLDH | Gluconobacter oxydans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | pyrroloquinoline quinine | Gluconobacter oxydans |