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Information on EC 1.1.1.369 - D-chiro-inositol 1-dehydrogenase and Organism(s) Bacillus subtilis and UniProt Accession P26935

for references in articles please use BRENDA:EC1.1.1.369
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IUBMB Comments
The enzyme, found in the bacterium Bacillus subtilis, also catalyses the reaction of EC 1.1.1.18, inositol 2-dehydrogenase, and can also use D-glucose and D-xylose. It shows trace activity with D-ribose and D-fructose . It is part of a myo-inositol/D-chiro-inositol degradation pathway leading to acetyl-CoA.
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This record set is specific for:
Bacillus subtilis
UNIPROT: P26935
The expected taxonomic range for this enzyme is: Bacteria
The taxonomic range for the selected organisms is: Bacillus subtilis
Synonyms
IDH, iolG, TM0414, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IDH
255309
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SYSTEMATIC NAME
IUBMB Comments
1D-chiro-inositol:NAD+ 1-oxidoreductase
The enzyme, found in the bacterium Bacillus subtilis, also catalyses the reaction of EC 1.1.1.18, inositol 2-dehydrogenase, and can also use D-glucose and D-xylose. It shows trace activity with D-ribose and D-fructose [1]. It is part of a myo-inositol/D-chiro-inositol degradation pathway leading to acetyl-CoA.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1D-chiro-inositol + NAD+
2D-2,3,5/4,6-pentahydroxycyclohexanone + NADH + H+
show the reaction diagram
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
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1D-chiro-inositol + NAD+
2D-2,3,5/4,6-pentahydroxycyclohexanone + NADH + H+
show the reaction diagram
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the enzyme is part of a myo-inositol/D-chiro-inositol degradation pathway leading to acetyl-CoA
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.4
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isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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enzyme forms part of the iol operon for myo-inositol catabolism, consisting of 10 iol genes, iolA to iolJ. iolG corresponds to idh, encoding myo-inositol 2-dehydrogenase. Disruption of the iol promoter prevents synthesis of the iol transcript as well as that of Idh. Immediately upstream of the iol operon, two genes iolR and iolS with divergent orientations to the iol operon are localized. Disruption of iolR but not iolS causes constitutive synthesis of the iol transcript and Idh. The iolRS genes are cotranscribed from another inositol-inducible promoter
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39000
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4 * 39000, SDS-PAGE
155000 - 160000
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sucrose density gradient centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 39000, SDS-PAGE
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
purified as a C-terminal His6 tag fusion protein
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as a C-terminal His6 tag fusion protein
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme synthesis is induced by myo-inositol
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enzyme synthesis is repressed by D-glucose
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ramaley, R.; Fujita, Y.; Freese, E.
Purification and properties of Bacillus subtilis inositol dehydrogenase
J. Biol. Chem.
254
7684-7690
1979
Bacillus subtilis (P26935), Bacillus subtilis 168 (P26935)
Manually annotated by BRENDA team
Yoshida, K.; Yamaguchi, M.; Morinaga, T.; Ikeuchi, M.; Kinehara, M.; Ashida, H.
Genetic modification of Bacillus subtilis for production of D-chiro-inositol, an investigational drug candidate for treatment of type 2 diabetes and polycystic ovary syndrome
Appl. Environ. Microbiol.
72
1310-1315
2006
Bacillus subtilis (P26935), Bacillus subtilis 168 (P26935)
Manually annotated by BRENDA team
Yoshida, K.I.; Aoyama, D.; Ishio, I.; Shibayama, T.; Fujita, Y.
Organization and transcription of the myo-inositol operon, iol, of Bacillus subtilis
J. Bacteriol.
179
4591-4598
1997
Bacillus subtilis 168 (P26935), Bacillus subtilis (P26935)
Manually annotated by BRENDA team
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