Difference between revisions of "PdhB"

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(Phenotypes of a mutant)
(Extended information on the protein)
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=== Extended information on the protein ===
 
=== Extended information on the protein ===
  
* '''Kinetic information:'''
+
* '''Kinetic information:''' Michaelis-Menten [http://www.ncbi.nlm.nih.gov/pubmed/6414463 PubMed]
  
 
* '''Domains:'''  
 
* '''Domains:'''  
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
 +
** Inhibited thiamine 2-thiothiazolone diphosphate and NADH [http://www.ncbi.nlm.nih.gov/pubmed/6414463 PubMed]
 +
** Low sensibility to NADPH
  
 
* '''Interactions:''' [[PdhA]]-[[PdhB]]-[[PdhC]]-[[PdhD]]
 
* '''Interactions:''' [[PdhA]]-[[PdhB]]-[[PdhC]]-[[PdhD]]

Revision as of 14:08, 10 June 2009

  • Description: pyruvate dehydrogenase (E1 beta subunit)

Gene name pdhB
Synonyms
Essential no
Product pyruvate dehydrogenase (E1 beta subunit)
Function links glycolysis and TCA cycle
MW, pI 35 kDa, 4.547
Gene length, protein length 975 bp, 325 aa
Immediate neighbours pdhA, pdhC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PdhB context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU14590

Phenotypes of a mutant

  • defects in sporulation and unable to grow on glucose as single carbon source PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: Michaelis-Menten PubMed
  • Domains:
  • Modification: phosphorylation on (Ser-302 OR Ser-306) PubMed
  • Cofactor(s):
  • Effectors of protein activity:
    • Inhibited thiamine 2-thiothiazolone diphosphate and NADH PubMed
    • Low sensibility to NADPH
  • Localization: membrane associated PubMed

Database entries

  • Structure: 1W88 (E1 in complex with subunit binding domain of E2, Geobacillus stearothermophilus)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: expression activated by glucose (2.8 fold) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP459 (spc), available in Stülke lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:

Labs working on this gene/protein

Arthur Aronson, Purdue University, West Lafayette, USA homepage

Your additional remarks

References

  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. Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 PubMed
  3. Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 PubMed
  4. Gao et al. (2002) The E1beta and E2 subunits of the Bacillus subtilis pyruvate dehydrogenase complex are involved in regulation of sporulation.J. Bacteriol. 184: 2780-2788. PubMed
  5. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed