IolG

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  • Description: inositol 2-dehydrogenase

Gene name iolG
Synonyms idh, iol
Essential no
Product inositol 2-dehydrogenase
Function myo-inositol catabolism
Gene expression levels in SubtiExpress: iolG
Metabolic function and regulation of this protein in SubtiPathways:
Sugar catabolism
MW, pI 38 kDa, 4.865
Gene length, protein length 1032 bp, 344 aa
Immediate neighbours iolH, iolF
Sequences Protein DNA DNA_with_flanks
Genetic context
Idh context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
IolG expression.png















Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

CcpA regulon, IolR regulon

The gene

Basic information

  • Locus tag: BSU39700

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH (according to Swiss-Prot)
  • Protein family: gfo/idh/mocA family (according to Swiss-Prot)

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Kosei Tanaka, Shintaro Tajima, Shinji Takenaka, Ken-ichi Yoshida
An improved Bacillus subtilis cell factory for producing scyllo-inositol, a promising therapeutic agent for Alzheimer's disease.
Microb Cell Fact: 2013, 12;124
[PubMed:24325193] [WorldCat.org] [DOI] (I e)

Hongyan Zheng, Drew Bertwistle, David A R Sanders, David R J Palmer
Converting NAD-specific inositol dehydrogenase to an efficient NADP-selective catalyst, with a surprising twist.
Biochemistry: 2013, 52(34);5876-83
[PubMed:23952058] [WorldCat.org] [DOI] (I p)

Karin E van Straaten, Hongyan Zheng, David R J Palmer, David A R Sanders
Structural investigation of myo-inositol dehydrogenase from Bacillus subtilis: implications for catalytic mechanism and inositol dehydrogenase subfamily classification.
Biochem J: 2010, 432(2);237-47
[PubMed:20809899] [WorldCat.org] [DOI] (I p)

Ken-ichi Yoshida, Masanori Yamaguchi, Tetsuro Morinaga, Masaki Kinehara, Maya Ikeuchi, Hitoshi Ashida, Yasutaro Fujita
myo-Inositol catabolism in Bacillus subtilis.
J Biol Chem: 2008, 283(16);10415-24
[PubMed:18310071] [WorldCat.org] [DOI] (P p)

K I Yoshida, T Shibayama, D Aoyama, Y Fujita
Interaction of a repressor and its binding sites for regulation of the Bacillus subtilis iol divergon.
J Mol Biol: 1999, 285(3);917-29
[PubMed:9887260] [WorldCat.org] [DOI] (P p)

K I Yoshida, D Aoyama, I Ishio, T Shibayama, Y Fujita
Organization and transcription of the myo-inositol operon, iol, of Bacillus subtilis.
J Bacteriol: 1997, 179(14);4591-8
[PubMed:9226270] [WorldCat.org] [DOI] (P p)

Y Fujita, K Shindo, Y Miwa, K Yoshida
Bacillus subtilis inositol dehydrogenase-encoding gene (idh): sequence and expression in Escherichia coli.
Gene: 1991, 108(1);121-5
[PubMed:1761221] [WorldCat.org] [DOI] (P p)

J Nihashi, Y Fujita
Catabolite repression of inositol dehydrogenase and gluconate kinase syntheses in Bacillus subtilis.
Biochim Biophys Acta: 1984, 798(1);88-95
[PubMed:6322857] [WorldCat.org] [DOI] (P p)

R Ramaley, Y Fujita, E Freese
Purification and properties of Bacillus subtilis inositol dehydrogenase.
J Biol Chem: 1979, 254(16);7684-90
[PubMed:112095] [WorldCat.org] (P p)