Difference between revisions of "PdhD"

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=References=
 
=References=
 
==Reviews==
 
==Reviews==
<pubmed> 19476487 9655937 2227213 6805383 10672230</pubmed>
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<pubmed> 19476487 9655937 2227213 6805383 10672230 22340847 </pubmed>
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==Original publications==
 
==Original publications==
 
<pubmed>12850135 6414463 11976308 17726680 20081037 20933603  24204596</pubmed>
 
<pubmed>12850135 6414463 11976308 17726680 20081037 20933603  24204596</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:35, 17 February 2014

  • 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
Gene expression levels in SubtiExpress: pdhD
Interactions involving this protein in SubtInteract: PdhD
Metabolic function and regulation of this protein in SubtiPathways:
pdhD
MW, pI 49 kDa, 4.76
Gene length, protein length 1410 bp, 470 aa
Immediate neighbours pdhC, slp
Sequences Protein DNA DNA_with_flanks
Genetic context
PdhD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PdhD expression.png















Categories containing this gene/protein

carbon core metabolism

This gene is a member of the following regulons

stringent response

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)

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

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:
  • FLAG-tag construct: GP1427 (spc, based on pGP1331), available in the Stülke lab

Labs working on this gene/protein

Your additional remarks

References

Reviews

J Prell, G Mulley, F Haufe, J P White, A Williams, R Karunakaran, J A Downie, P S Poole
The PTS(Ntr) system globally regulates ATP-dependent transporters in Rhizobium leguminosarum.
Mol Microbiol: 2012, 84(1);117-29
[PubMed:22340847] [WorldCat.org] [DOI] (I p)

Kai Tittmann
Reaction mechanisms of thiamin diphosphate enzymes: redox reactions.
FEBS J: 2009, 276(9);2454-68
[PubMed:19476487] [WorldCat.org] [DOI] (I p)

K F Sheu, J P Blass
The alpha-ketoglutarate dehydrogenase complex.
Ann N Y Acad Sci: 1999, 893;61-78
[PubMed:10672230] [WorldCat.org] [DOI] (P 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