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
Gene expression levels in SubtiExpress: pdhC
Interactions involving this protein in SubtInteract: PdhC
Metabolic function and regulation of this protein in SubtiPathways: pdhC
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

carbon core metabolism, membrane proteins, most abundant 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

• BsubCyc: BSU14600

• 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): AcoC, BkdB, OdhB

Extended information on the protein

• Kinetic information: Michaelis-Menten PubMed

• Domains:

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

• Cofactors:
  • lipoic acid

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

• Interactions:
  • PdhA-PdhB-PdhC-PdhD

• Localization: membrane associated PubMed

Database entries

• BsubCyc: BSU14600

• 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

• Expression browser: pdhC 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
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 11281 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 33899 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 10012 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 6860 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 6154 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)