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Literature summary for 1.1.1.369 extracted from

  • Ramaley, R.; Fujita, Y.; Freese, E.
    Purification and properties of Bacillus subtilis inositol dehydrogenase (1979), J. Biol. Chem., 254, 7684-7690.
    View publication on PubMed
Search for more literature for 1.1.1.369

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39000
-
 4 * 39000, SDS-PAGE Bacillus subtilis
155000 160000 sucrose density gradient centrifugation Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P26935
-
-
Bacillus subtilis 168 P26935
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme can remove only the single equatorial hydrogen of the cyclitol or pyranose ring. Inositol dehydrogenase requires NAD+ and does not react with 2-deoxy-D-glucose or scyllo-inositol. Enzyme also functions as inositol dehydrogenase and accepts alpha-D-glucose and D-xylose Bacillus subtilis ?
-
 ?
additional information the enzyme can remove only the single equatorial hydrogen of the cyclitol or pyranose ring. Inositol dehydrogenase requires NAD+ and does not react with 2-deoxy-D-glucose or scyllo-inositol. Enzyme also functions as inositol dehydrogenase and accepts alpha-D-glucose and D-xylose Bacillus subtilis 168 ?
-
 ?

Subunits

Subunits Comment Organism
tetramer 4 * 39000, SDS-PAGE Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Bacillus subtilis

pI Value

Organism Comment pI Value Maximum pI Value
Bacillus subtilis isoelectric focusing
-
 4.4

Expression

Organism Comment Expression
Bacillus subtilis enzyme synthesis is repressed by D-glucose down
Bacillus subtilis enzyme synthesis is induced by myo-inositol up