Difference between revisions of "PdhD"

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(References)
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** Low sensibility to NADPH [http://www.ncbi.nlm.nih.gov/pubmed/6414463 PubMed]
 
** Low sensibility to NADPH [http://www.ncbi.nlm.nih.gov/pubmed/6414463 PubMed]
  
* '''Interactions:''' [[OdhA]]-[[OdhB]]-[[PdhD]][[PdhA]]-[[PdhB]]-[[PdhC]]-[[PdhD]]
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* '''Interactions:'''  
 +
** [[OdhA]]-[[OdhB]]-[[PdhD]] {{PubMed|20933603}}
 +
** [[PdhA]]-[[PdhB]]-[[PdhC]]-[[PdhD]]
  
 
* '''Localization:''' cytoplasm (according to Swiss-Prot)
 
* '''Localization:''' cytoplasm (according to Swiss-Prot)
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<pubmed> 19476487 9655937 2227213 6805383 </pubmed>
 
<pubmed> 19476487 9655937 2227213 6805383 </pubmed>
 
==Original publications==
 
==Original publications==
<pubmed>12850135 6414463 11976308 17726680 20081037 </pubmed>
+
<pubmed>12850135 6414463 11976308 17726680 20081037 20933603</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 08:05, 13 October 2010

  • Description: dihydrolipoamide dehydrogenase E3 subunit of both pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes

Gene name pdhD
Synonyms citL
Essential no
Product dihydrolipoamide dehydrogenase E3 subunit
of both pyruvate dehydrogenase and 2-oxoglutarate
dehydrogenase complexes
Function links glycolysis and TCA cycle, enzyme in TCA cycle
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 49 kDa, 4.76
Gene length, protein length 1410 bp, 470 aa
Immediate neighbours pdhC, slp
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PdhD context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU14610

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: Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH (according to Swiss-Prot)
  • Protein family: class-I pyridine nucleotide-disulfide oxidoreductase family (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 PubMed
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure: 1EBD (complex with binding domain of dihydrolipoamide acetylase, Geobacillus stearothermophilus), 1EBD (complex with binding domain of dihydrolipoamide acetylase, Geobacillus stearothermophilus)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • pdhA: expression activated by glucose (2.0-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:
  • Expression vector:
  • lacZ fusion: pGP723 (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

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