Difference between revisions of "Icd"

From SubtiWiki
Jump to: navigation, search
(Biological materials)
(Extended information on the protein)
Line 61: Line 61:
 
=== Extended information on the protein ===
 
=== Extended information on the protein ===
  
* '''Kinetic information:'''
+
* '''Kinetic information:''' Reversible Michaelis-Menten [http://www.ncbi.nlm.nih.gov/pubmed/4147570 PubMed]
  
 
* '''Domains:'''  
 
* '''Domains:'''  
Line 70: Line 70:
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
 +
** Inhibited by glyoxylate, oxaloacetate and oxalomalate [http://www.ncbi.nlm.nih.gov/pubmed/4147570 PubMed]
 +
*** Better inhibition when glyoxylate and oxaloacetate is combined, probably due to the non-enzymatic conversion into oxalomalate, which is a strong inhibitor [http://www.ncbi.nlm.nih.gov/pubmed/4147570 PubMed]
  
 
* '''Interactions:'''
 
* '''Interactions:'''

Revision as of 15:21, 10 June 2009

  • Description: isocitrate dehydrogenase

Gene name icd
Synonyms citC
Essential no
Product isocitrate dehydrogenase
Function TCA cycle
MW, pI 46 kDa, 4.833
Gene length, protein length 1269 bp, 423 aa
Immediate neighbours citZ, mdh
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Icd context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU29130

Phenotypes of a mutant

reduced ability to sporulate PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH (according to Swiss-Prot)
  • Protein family: isocitrate and isopropylmalate dehydrogenases family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: Reversible Michaelis-Menten PubMed
  • Domains:
  • Cofactor(s):
  • Effectors of protein activity:
    • Inhibited by glyoxylate, oxaloacetate and oxalomalate PubMed
      • Better inhibition when glyoxylate and oxaloacetate is combined, probably due to the non-enzymatic conversion into oxalomalate, which is a strong inhibitor PubMed
  • Interactions:
  • Localization: attached to the membrane PubMed

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: repressed by glucose (2.2-fold) (CcpA) PubMed, citZ: catabolite repression (CcpA), repression by glucose + glutamate (CcpC)

icd: constitutive

  • Regulatory mechanism: CcpA: transcription repression
  • Additional information:

Biological materials

  • Mutant: GP666 (spc), GP672 (erm), available in Stülke lab
  • Expression vector:
    • pGP1121 (N-terminal Strep-tag, for SPINE, purification from B. subtilis, in pGP380) (available in Stülke lab)
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab

Labs working on this gene/protein

[Linc Sonenshein|Linc Sonenshein]], Tufts University, Boston, MA, USA Homepage

Your additional remarks

References

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

Satinder K Singh, Stephen P Miller, Antony Dean, Leonard J Banaszak, David C LaPorte
Bacillus subtilis isocitrate dehydrogenase. A substrate analogue for Escherichia coli isocitrate dehydrogenase kinase/phosphatase.
J Biol Chem: 2002, 277(9);7567-73
[PubMed:11751849] [WorldCat.org] [DOI] (P p)

K Matsuno, T Blais, A W Serio, T Conway, T M Henkin, A L Sonenshein
Metabolic imbalance and sporulation in an isocitrate dehydrogenase mutant of Bacillus subtilis.
J Bacteriol: 1999, 181(11);3382-91
[PubMed:10348849] [WorldCat.org] [DOI] (P p)

  1. Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways. Metab Eng. 5: 133-149 PubMed
  2. Matsuno K, Blais T, Serio AW, Conway T, Henkin TM, Sonenshein AL (1999) Metabolic imbalance and sporulation in an isocitrate dehydrogenase mutant of Bacillus subtilis. J Bacteriol 181:3382-3391. PubMed
  3. Singh SK, Miller SP, Dean A, Banaszak LJ, LaPorte DC (2002) Bacillus subtilis isocitrate dehydrogenase. A substrate analogue for Escherichia coli isocitrate dehydrogenase kinase/ phosphatase. J Biol Chem 277: 7567-7573. PubMed
  4. Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 PubMed
  5. Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
  6. Levine et al. (2006) Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes. Proteomics 6, 2157-2173. PubMed
  7. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed