PdhC

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  • Description: pyruvate dehydrogenase (dihydrolipoamide acetyltransferase E2 subunit)

Gene name pdhC
Synonyms
Essential no
Product pyruvate dehydrogenase
(dihydrolipoamide acetyltransferase E2 subunit)
Function links glycolysis and TCA cycle
Gene expression levels in SubtiExpress: pdhC
Interactions involving this protein in SubtInteract: PdhC
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 47 kDa, 4.855
Gene length, protein length 1326 bp, 442 aa
Immediate neighbours pdhB, pdhD
Sequences Protein DNA DNA_with_flanks
Genetic context
PdhC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PdhC expression.png















Categories containing this gene/protein

carbon core metabolism, membrane proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU14600

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: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine (according to Swiss-Prot)
  • Protein family: lipoyl-binding domain (according to Swiss-Prot)

Extended information on the protein

  • Kinetic information: Michaelis-Menten PubMed
  • Domains:
  • Modification: phosphorylated (Ser/Thr/Tyr) PubMed
  • Cofactor(s):
    • lipoic acid
  • Effectors of protein activity:
    • Inhibited by 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), 2PDE (peripheral subunit binding domain, Geobacillus stearothermophilus), 1LAC (lipoyl domain, Geobacillus stearothermophilus), 1B5S (catalytic domain (residues 184-425) , Geobacillus stearothermophilus)
  • UniProt: P21883
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • pdhA: expression activated by glucose (1.9-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:
  • Expression vector:
  • lacZ fusion:
  • 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)

L C Packman, D S Hipps
The structural domains in the E2 component of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus.
Biochem Soc Trans: 1991, 19(4);917-22
[PubMed:1794583] [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