Q8NTE1 · DLDH_CORGL

Function

function

Lipoamide dehydrogenase is an essential component of the pyruvate dehydrogenase (PDH) and 2-oxoglutarate dehydrogenase (ODH) complexes. Catalyzes the reoxidation of dihydrolipoyl groups which are covalently attached to the lipoate acyltransferase components (E2) of the complexes. Also catalyzes a reversible NADH:NAD+ transhydrogenation, and is able to transfer electrons from NADH to various redox-active compounds and quinones. May be involved in quinone redox cycling in C.glutamicum.

Miscellaneous

The active site is a redox-active disulfide bond.
Overexpression of LPD enhances sensitivity to menadione, but has no effect on sensitivity to paraquat or hydrogen peroxide.

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.636 μMlipoate

pH Dependence

Optimum pH is 7.0-7.5 for the reduction of lipoate by NADH.

Temperature Dependence

Optimum temperature is 50 degrees Celsius for the reduction of lipoate by NADH.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site34-42FAD (UniProtKB | ChEBI)
Binding site51FAD (UniProtKB | ChEBI)
Binding site114FAD (UniProtKB | ChEBI)
Binding site179-183NAD+ (UniProtKB | ChEBI)
Binding site202NAD+ (UniProtKB | ChEBI)
Binding site269-272NAD+ (UniProtKB | ChEBI)
Binding site312FAD (UniProtKB | ChEBI)
Binding site320FAD (UniProtKB | ChEBI)
Active site448Proton acceptor

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functiondihydrolipoyl dehydrogenase activity
Molecular Functionflavin adenine dinucleotide binding
Biological Processtricarboxylic acid cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dihydrolipoyl dehydrogenase
  • EC number
  • Short names
    LPD
  • Alternative names
    • Dihydrolipoamide dehydrogenase
    • E3 component of alpha-ketoacid dehydrogenase complexes

Gene names

    • Name
      lpd
    • Ordered locus names
      Cgl0366, cg0441

Organism names

Accessions

  • Primary accession
    Q8NTE1
  • Secondary accessions
    • Q6M7Z6
    • Q9Z466

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, chain, disulfide bond.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00004205232-469Dihydrolipoyl dehydrogenase
Disulfide bond42↔47Redox-active

Keywords

Interaction

Subunit

Homodimer (By similarity).
Part of an unusual ODH/PDH supercomplex, consisting of AceE (E1), AceF (E2), and Lpd (E3) together with OdhA (E1+E2)

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    469
  • Mass (Da)
    50,652
  • Last updated
    2002-10-01 v1
  • Checksum
    7F8FFE6B510B8725
MTEHYDVVVLGAGPGGYVSAIRAAQLGKKVAVIEKQYWGGVCLNVGCIPSKSLIKNAEVAHTFTHEKKTFGINGEVTFNYEDAHKRSRGVSDKIVGGVHYLMKKNKIIEIHGLGNFKDAKTLEVTDGKDAGKTITFDDCIIATGSVVNTLRGVDFSENVVSFEEQILNPVAPKKMVIVGAGAIGMEFAYVLGNYGVDVTVIEFMDRVLPNEDAEVSKVIAKAYKKMGVKLLPGHATTAVRDNGDFVEVDYQKKGSDKTETLTVDRVMVSVGFRPRVEGFGLENTGVKLTERGAIEIDDYMRTNVDGIYAIGDVTAKLQLAHVAEAQGIVAAETIAGAETQTLGDYMMMPRATFCNPQVSSFGYTEEQAKEKWPDREIKVASFPFSANGKAVGLAETDGFAKIVADAEFGELLGAHLVGANASELINELVLAQNWDLTTEEISRSVHIHPTLSEAVKEAAHGISGHMINF

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict382in Ref. 1; CAA76340

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Y16642
EMBL· GenBank· DDBJ
CAA76340.1
EMBL· GenBank· DDBJ
Genomic DNA
BA000036
EMBL· GenBank· DDBJ
BAB97759.1
EMBL· GenBank· DDBJ
Genomic DNA
BX927149
EMBL· GenBank· DDBJ
CAF19080.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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