PdhB

• Description: pyruvate dehydrogenase (E1 beta subunit)
  
  

Gene name	pdhB
Synonyms
Essential	no
Product	pyruvate dehydrogenase (E1 beta subunit)
Function	links glycolysis and TCA cycle
Interactions involving this protein in SubtInteract: PdhB
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	35 kDa, 4.547
Gene length, protein length	975 bp, 325 aa
Immediate neighbours	pdhA, pdhC
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

carbon core metabolism, membrane proteins, phosphoproteins

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]

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:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information: Michaelis-Menten PubMed

• Domains:

• Modification: phosphorylation on (Ser-302 OR Ser-306) 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)

• UniProt: P21882

• KEGG entry: [3]

• E.C. number: 1.2.4.1

Expression and regulation

• Operon: pdhA-pdhB-pdhC-pdhD PubMed

• Expression browser: pdhB PubMed

• Sigma factor: SigA PubMed

• 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

• Additional information:

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

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)