pyruvate dehydrogenase (dihydrolipoamide acetyltransferase E2 subunit)
function
links glycolysis and TCA cycle
product
pyruvate dehydrogenase
(dihydrolipoamide acetyltransferase E2 subunit)
Genomic Context
categories
[category|SW 2|Metabolism] → [category|SW 2.2|Carbon metabolism] → [category|SW 2.2.1|Carbon core metabolism] → [category|SW 2.2.1.4|TCA cycle][category|SW 3|Information processing] → [category|SW 3.1|Genetics] → [category|SW 3.1.9|Newly identified competence genes][category|SW 6|Groups of genes] → [category|SW 6.2|Membrane proteins][SW|Categories] containing this gene/protein
[SW|carbon core metabolism], [SW|membrane proteins], [SW|most abundant proteins]This gene is a member of the following [SW|regulons]
[SW|stringent response]Gene
Coordinates on the chromosome (coding sequence)
1,530,537 -> 1,531,865
Phenotypes of a mutant
defects in sporulation and unable to grow on glucose as single carbon source [Pubmed|11976308]The protein
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)
[protein|search|AcoC], [protein|search|BkdB], [protein|search|OdhB]Kinetic information
Michaelis-Menten [Pubmed|6414463]Modification
phosphorylated (Ser/Thr/Tyr) [Pubmed|17726680][SW|Cofactors]
lipoic acidEffectors of protein activity
Inhibited by thiamine 2-thiothiazolone diphosphate and NADH [Pubmed|6414463]Low sensibility to NADPHStructure
[PDB|1W88] (E1 in complex with subunit binding domain of E2, ''Geobacillus stearothermophilus''), [PDB|2PDE] (peripheral subunit binding domain, ''Geobacillus stearothermophilus''), [PDB|1LAC] (lipoyl domain, ''Geobacillus stearothermophilus''), [PDB|1B5S] (catalytic domain (residues 184-425) , ''Geobacillus stearothermophilus'')[SW|Localization]
membrane associated [Pubmed|18763711]cytoplasm (homogeneously distributed throughout the cell) [Pubmed|24825009][SW|Interactions]
[protein|search|PdhA]-[protein|search|PdhB]-[protein|search|PdhC]-[protein|search|PdhD]Expression and Regulation
Operon
''[protein|search|pdhA]-[protein|search|pdhB]-[protein|search|pdhC]-[protein|search|pdhD]'' [Pubmed|11976308]''[protein|search|pdhC]-[protein|search|pdhD]'' [Pubmed|11976308][SW|Sigma factor]
''[protein|search|pdhA]'': [protein|search|SigA] [Pubmed|20081037]''[protein|search|pdhC]'': [protein|search|SigA] [Pubmed|11976308]Regulation
''[protein|search|pdhA]'': expression activated by glucose (1.9-fold) [Pubmed|12850135]subject to negative stringent control upon amino acid limitation [Pubmed|20081037]Additional information
belongs to the 100 [SW|most abundant proteins] [PubMed|15378759]Labs working on this gene/protein
[SW|Arthur Aronson], Purdue University, West Lafayette, USA [http://wwwdev.gradschool.purdue.edu/PULSe/faculty.cfm?fid=5&range=0 homepage]References
Reviews
19476487,9655937,2227213,6805383,1794583,24798336 Original publications
9352926,24825009,9352926,17726680,12850135,18763711,6414463,11976308,20081037,22862776,15378759