dihydrolipoamide dehydrogenase E3 subunit of both pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
function
links glycolysis and TCA cycle, enzyme in TCA cycle
product
dihydrolipoamide dehydrogenase E3 subunit
of both pyruvate dehydrogenase and 2-oxoglutarate
dehydrogenase complexes
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 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.8|Phosphorylation on either a Ser, Thr or Tyr residue][SW|Categories] containing this gene/protein
[SW|carbon core metabolism], [SW|most abundant proteins]This gene is a member of the following [SW|regulons]
[SW|stringent response]Gene
Coordinates on the chromosome (coding sequence)
1,531,870 -> 1,533,282
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
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)
[protein|search|AcoL], [protein|search|LpdV]Kinetic information
Michaelis-Menten [Pubmed|6414463]Modification
phosphorylated (Ser/Thr/Tyr) [Pubmed|17726680]Effectors of protein activity
Inhibited thiamine 2-thiothiazolone diphosphate and NADH [Pubmed|6414463]Low sensibility to NADPH [Pubmed|6414463]Structure
[PDB|1EBD] (complex with binding domain of dihydrolipoamide acetylase, Geobacillus stearothermophilus), [PDB|1EBD] (complex with binding domain of dihydrolipoamide acetylase, ''Geobacillus stearothermophilus'')[SW|Localization]
cytoplasm (according to Swiss-Prot)[SW|Interactions]
[protein|search|OdhA]-[protein|search|OdhB]-[protein|search|PdhD] [Pubmed|20933603][protein|search|PdhA]-[protein|search|PdhB]-[protein|search|PdhC]-[protein|search|PdhD]Expression and Regulation
[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 (2.0-fold) [Pubmed|12850135]subject to negative stringent control upon amino acid limitation [Pubmed|20081037]Regulatory mechanism
stringent response: due to presence of guanine at 1 position of the transcript [Pubmed|20081037]Additional information
belongs to the 100 [[most abundant proteins]] [PubMed|15378759]Biological materials
lacZ fusion
pGP723 (in [protein|search|pAC5]), available in [SW|Stülke] labtwo-hybrid system
''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW|Stülke] labFLAG-tag construct
GP1427 (spc, based on [SW|pGP1331]), available in the [SW|Stülke] labAntibody
**References
Reviews
19476487,9655937,2227213,6805383,10672230,24798336 Original publications
12850135,6414463,11976308,17726680,20081037,20933603,24204596,15378759