Difference between revisions of "PdhB"

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(Biological materials)
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* '''Operon:''' ''[[pdhA]]-[[pdhB]]-[[pdhC]]-[[pdhD]]'' {{PubMed|11976308}}
 
* '''Operon:''' ''[[pdhA]]-[[pdhB]]-[[pdhC]]-[[pdhD]]'' {{PubMed|11976308}}
  
* '''Sigma factor:''' [[SigA]] {{PubMed|11976308}}
+
* '''Sigma factor:''' [[SigA]] {{PubMed|20081037}}
  
* '''Regulation:''' expression activated by glucose (2.8 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
+
* '''Regulation:'''  
 +
** expression activated by glucose (2.8-fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
 +
** subject to negative stringent control upon amino acid limitation {{PubMed|20081037}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
 +
** stringent response: due to presence of guanine at +1 position of the transcript {{PubMed|20081037}}
  
 
* '''Additional information:'''
 
* '''Additional information:'''

Revision as of 18:51, 19 January 2010

  • Description: pyruvate dehydrogenase (E1 beta subunit)

Gene name pdhB
Synonyms
Essential no
Product pyruvate dehydrogenase (E1 beta subunit)
Function links glycolysis and TCA cycle
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
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
    • subject to negative stringent control upon amino acid limitation PubMed
  • Regulatory mechanism:
    • stringent response: due to presence of guanine at +1 position of the transcript PubMed
  • Additional information:

Biological materials

  • Mutant: GP459 (spc), available in Stülke lab
  • Expression vector:
  • lacZ fusion: pGP722 (in pAC5), available in Stülke lab
  • 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