PdhC

• 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
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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

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]

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)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information: Michaelis-Menten PubMed

• Domains:

• Modification: phosphorylated (Ser/Thr/Tyr) PubMed

• Cofactor(s):

• Effectors of protein activity:
  • Inhibited thiamine 2-thiothiazolone diphosphate and NADH PubMed
  • Low sensibility to NADPH

• Interactions: PdhA-PdhB-PdhC-PdhD

• Localization: membrane associated PubMed

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]

• E.C. number: 2.3.1.12 2

Expression and regulation

• Operon:
  • pdhA-pdhB-pdhC-pdhD PubMed
  • pdhC-pdhD PubMed

• Sigma factor:
  • pdhA: SigA PubMed
  • pdhC: SigA PubMed

• 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

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)