Difference between revisions of "PdhB"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU14590&redirect=T BSU14590]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/pdhABCD.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/pdhABCD.html]
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU14590&redirect=T BSU14590]
  
 
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1W88 1W88] (E1 in complex with subunit binding domain of E2, ''Geobacillus stearothermophilus'')
 
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1W88 1W88] (E1 in complex with subunit binding domain of E2, ''Geobacillus stearothermophilus'')

Revision as of 13:36, 2 April 2014

  • Description: pyruvate dehydrogenase (E1 beta subunit)

Gene name pdhB
Synonyms
Essential no
Product pyruvate dehydrogenase (E1 beta subunit)
Function links glycolysis and TCA cycle
Gene expression levels in SubtiExpress: pdhB
Interactions involving this protein in SubtInteract: PdhB
Metabolic function and regulation of this protein in SubtiPathways:
pdhB
MW, pI 35 kDa, 4.547
Gene length, protein length 975 bp, 325 aa
Immediate neighbours pdhA, pdhC
Sequences Protein DNA DNA_with_flanks
Genetic context
PdhB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PdhB expression.png















Categories containing this gene/protein

carbon core metabolism, membrane proteins, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

stringent response

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:

Extended information on the protein

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

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

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

Reviews

Original publications