Difference between revisions of "PdhA"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 5117 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 5117 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 18311 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 18311 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4425 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 5452 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 7055 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 14:11, 17 April 2014

  • Description: pyruvate dehydrogenase (E1 alpha subunit)

Gene name pdhA
Synonyms aceA
Essential yes
Product pyruvate dehydrogenase (E1 alpha subunit)
Function links glycolysis and TCA cycle
Gene expression levels in SubtiExpress: pdhA
Interactions involving this protein in SubtInteract: PdhA
Metabolic function and regulation of this protein in SubtiPathways:
pdhA
MW, pI 41 kDa, 5.837
Gene length, protein length 1113 bp, 371 aa
Immediate neighbours ykyA, pdhB
Sequences Protein DNA DNA_with_flanks
Genetic context
PdhA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PdhA expression.png















Categories containing this gene/protein

carbon core metabolism, essential genes, most abundant proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU14580

Phenotypes of a mutant

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:
  • 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 (3.4) 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:
    • The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 5117 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 18311 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4425 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 5452 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 7055 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Arthur Aronson, Purdue University, West Lafayette, USA homepage

Your additional remarks

References

Reviews

Kai Tittmann
Reaction mechanisms of thiamin diphosphate enzymes: redox reactions.
FEBS J: 2009, 276(9);2454-68
[PubMed:19476487] [WorldCat.org] [DOI] (I p)

U Neveling, S Bringer-Meyer, H Sahm
Gene and subunit organization of bacterial pyruvate dehydrogenase complexes.
Biochim Biophys Acta: 1998, 1385(2);367-72
[PubMed:9655937] [WorldCat.org] [DOI] (P p)

M S Patel, T E Roche
Molecular biology and biochemistry of pyruvate dehydrogenase complexes.
FASEB J: 1990, 4(14);3224-33
[PubMed:2227213] [WorldCat.org] [DOI] (P p)

P A Frey
Mechanism of coupled electron and group transfer in Escherichia coli pyruvate dehydrogenase.
Ann N Y Acad Sci: 1982, 378;250-64
[PubMed:6805383] [WorldCat.org] [DOI] (P p)

Original publications