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Literature summary 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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.18 0.23
-
NAD+
-
Bacillus subtilis
1.1.1.18 18
-
myo-inositol
-
Bacillus subtilis
1.1.1.18 56
-
alpha-D-glucose
-
Bacillus subtilis
1.1.1.18 167
-
D-glucose
-
Bacillus subtilis
1.1.1.18 190
-
D-xylose
-
Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.18 39000
-
4 * 39000, SDS-PAGE Bacillus subtilis
1.1.1.18 160000
-
gel filtration Bacillus subtilis
1.1.1.369 39000
-
4 * 39000, SDS-PAGE Bacillus subtilis
1.1.1.369 155000 160000 sucrose density gradient centrifugation Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.18 myo-inositol + NAD+ Bacillus subtilis
-
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.18 Bacillus subtilis
-
-
-
1.1.1.369 Bacillus subtilis P26935
-
-
1.1.1.369 Bacillus subtilis 168 P26935
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.18 to homogeneity, chromatography steps Bacillus subtilis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.18 cell culture
-
Bacillus subtilis
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.18 34.3
-
-
Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.18 alpha-D-glucopyranose + NAD+ 4fold lower activity compared to myo-inositol as substrate, does not act with the beta-anomer Bacillus subtilis D-gluconate + NADH
-
?
1.1.1.18 D-glucose + NAD+
-
Bacillus subtilis D-gluconate + NADH
-
?
1.1.1.18 D-xylose + NAD+ very low activity Bacillus subtilis ? + NADH
-
?
1.1.1.18 myo-inositol + NAD+
-
Bacillus subtilis 2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
?
1.1.1.369 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 ?
-
?
1.1.1.369 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

EC Number Subunits Comment Organism
1.1.1.18 tetramer 4 * 39000, SDS-PAGE Bacillus subtilis
1.1.1.369 tetramer 4 * 39000, SDS-PAGE Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.18 9.5
-
-
Bacillus subtilis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.18 6.5
-
optimal pH-value for stability Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.18 NAD+
-
Bacillus subtilis
1.1.1.369 NAD+
-
Bacillus subtilis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.1.1.369 Bacillus subtilis isoelectric focusing
-
4.4

Expression

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