1.1.1.370: scyllo-inositol 2-dehydrogenase (NAD+)
This is an abbreviated version!
For detailed information about scyllo-inositol 2-dehydrogenase (NAD+), go to the full flat file.
Word Map on EC 1.1.1.370
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1.1.1.370
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myo-inositols
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stereoisomer
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scyllo-inosose
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repressor
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gymnema
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terrae
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burkholderia
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paracoccus
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casei
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l-glucose
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honeydew
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lactobacillus
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nicotinamide
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1-dehydrogenase
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honey
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stereoselectively
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sylvestre
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2-deoxy-scyllo-inosose
- 1.1.1.370
- myo-inositols
-
stereoisomer
- scyllo-inosose
- repressor
-
gymnema
-
terrae
-
burkholderia
-
paracoccus
-
casei
- l-glucose
-
honeydew
- lactobacillus
- nicotinamide
-
1-dehydrogenase
- honey
-
stereoselectively
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sylvestre
- 2-deoxy-scyllo-inosose
Reaction
Synonyms
DegA, IgdA, IolX, LgdA, NAD+-dependent SI dehydrogenase, Pl-scyllo-IDH, scyllo-inositol dehydrogenase, yisS
ECTree
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General Information
General Information on EC 1.1.1.370 - scyllo-inositol 2-dehydrogenase (NAD+)
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evolution
the enzyme belongs to the glucose-fructose oxidase/inositol dehydrogenase/microbial rhizopine-catabolizing (GFO/IDH/MocA) family
malfunction
metabolism
physiological function
additional information
inactivation of iolX impairs growth with scyllo-inositol as the carbon source
malfunction
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inactivation of iolX impairs growth with scyllo-inositol as the carbon source
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scyllo-inositol dehydrogenase is involved in the first step in the pathway that oxidizes L-glucose to produce L-glucono-1,5-lactone with concomitant reduction of NAD+ dependent manner
metabolism
the enzyme is involved in the inositol metabolic pathway in Bacillus subtilis, organization of the relevant genes, overview
metabolism
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the enzyme is involved in the inositol metabolic pathway in Bacillus subtilis, organization of the relevant genes, overview
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the enzyme is part of a scyllo-inositol degradation pathway leading to acetyl-CoA
physiological function
Bacillus subtilis is able to utilize at least three inositol stereoisomers as carbon sources, myo-, scyllo-, and D-chiro-inositol (MI, SI, and DCI, respectively). NAD+-dependent SI dehydrogenase is responsible for SI catabolism. IolQ is a transcriptional repressor of iolX. Expression of gene iolQ is required to regulate gene iolX transcription in response to scyllo-inositol, identification of the two IolQ-binding sites within the iolX promoter region
physiological function
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the enzyme is part of a scyllo-inositol degradation pathway leading to acetyl-CoA
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physiological function
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Bacillus subtilis is able to utilize at least three inositol stereoisomers as carbon sources, myo-, scyllo-, and D-chiro-inositol (MI, SI, and DCI, respectively). NAD+-dependent SI dehydrogenase is responsible for SI catabolism. IolQ is a transcriptional repressor of iolX. Expression of gene iolQ is required to regulate gene iolX transcription in response to scyllo-inositol, identification of the two IolQ-binding sites within the iolX promoter region
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in addition to the conserved catalytic residues (Lys106, Asp191, and His195), another residue, His318, located in the loop region of the adjacent subunit, is involved in substrate recognition. The Arg178 residue located in the flexible loop at the entrance of the catalytic site is also involved in substrate recognition, and plays an important role in accepting both L-glucose and inositols as substrates. The corresponding distances in the myo-inositol and scyllo-inosose complexes are 2.8 A and 3.1 A, respectively, and the relative positions of NAD+ and the inositols are the same as those seen in the lactone complex
additional information
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in addition to the conserved catalytic residues (Lys106, Asp191, and His195), another residue, His318, located in the loop region of the adjacent subunit, is involved in substrate recognition. The Arg178 residue located in the flexible loop at the entrance of the catalytic site is also involved in substrate recognition, and plays an important role in accepting both L-glucose and inositols as substrates. The corresponding distances in the myo-inositol and scyllo-inosose complexes are 2.8 A and 3.1 A, respectively, and the relative positions of NAD+ and the inositols are the same as those seen in the lactone complex