Difference between revisions of "IolG"

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=References=
 
=References=
  
<pubmed>18310071 112095, </pubmed>
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<pubmed>9887260,18310071 112095, </pubmed>
  
 
# Yoshida K, Yamaguchi M, Morinaga T, Kinehara M, Ikeuchi M, Ashida H, Fujita Y. (2008) myo-Inositol catabolism in Bacillus subtilis. ''J Biol Chem. '' ''' Apr 18;283(16):''' 10415-24. [http://www.ncbi.nlm.nih.gov/sites/entrez/18310071 PubMed]
 
# Yoshida K, Yamaguchi M, Morinaga T, Kinehara M, Ikeuchi M, Ashida H, Fujita Y. (2008) myo-Inositol catabolism in Bacillus subtilis. ''J Biol Chem. '' ''' Apr 18;283(16):''' 10415-24. [http://www.ncbi.nlm.nih.gov/sites/entrez/18310071 PubMed]
 
# Ramaley R, Fujita Y, Freese E. (1979) Purification and properties of Bacillus subtilis inositol dehydrogenase. ''J Biol Chem.'' '''Aug 25;254(16):''' 7684-90. [http://www.ncbi.nlm.nih.gov/sites/entrez/112095 PubMed]
 
# Ramaley R, Fujita Y, Freese E. (1979) Purification and properties of Bacillus subtilis inositol dehydrogenase. ''J Biol Chem.'' '''Aug 25;254(16):''' 7684-90. [http://www.ncbi.nlm.nih.gov/sites/entrez/112095 PubMed]

Revision as of 12:21, 12 June 2009

  • Description: inositol 2-dehydrogenase

Gene name iolG
Synonyms idh, iol
Essential no
Product inositol 2-dehydrogenase
Function myo-inositol catabolism
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
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Idh context.gif
This image was kindly provided by SubtiList





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)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization:

Database entries

  • Structure:
  • 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

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)

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)


  1. Yoshida K, Yamaguchi M, Morinaga T, Kinehara M, Ikeuchi M, Ashida H, Fujita Y. (2008) myo-Inositol catabolism in Bacillus subtilis. J Biol Chem. Apr 18;283(16): 10415-24. PubMed
  2. Ramaley R, Fujita Y, Freese E. (1979) Purification and properties of Bacillus subtilis inositol dehydrogenase. J Biol Chem. Aug 25;254(16): 7684-90. PubMed