PDPR
Identifiers
Aliases	PDPR, PDP3, pyruvate dehydrogenase phosphatase regulatory subunit
External IDs	OMIM: 617835 MGI: 2442188 HomoloGene: 9948 GeneCards: PDPR
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16q22.1 Start 70,114,332 bp[1] End 70,162,537 bp[1]
Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8|8 E1 Start 111,821,262 bp[2] End 111,863,706 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Top expressed in More reference expression data BioGPS n/a
Gene ontology Molecular function Cellular component Biological process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 55066 319518 Ensembl ENSG00000090857 ENSMUSG00000033624 UniProt Q8NCN5 Q7TSQ8 RefSeq (mRNA) NM_017990 NM_001322117 NM_001322118 NM_001322119 NM_198308 RefSeq (protein) NP_001309046 NP_001309047 NP_001309048 NP_060460 NP_938050 Location (UCSC) Chr 16: 70.11 – 70.16 Mb Chr 8: 111.82 – 111.86 Mb PubMed search [3] [4]
Wikidata
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Pyruvate dehydrogenase phosphatase regulatory subunit is a protein that in humans is encoded by the PDPR gene.^[5]

Structure[edit]

The complete cDNA of PDPR, which contains 2885 base pairs, has an open reading frame of 2634 nucleotides encoding a putative presequence of 31 amino acid residues and a mature protein of 847. Characteristics of native PDPR include ability to decrease the sensitivity of the catalytic subunit to Mg2+, and reversal of this inhibitory effect by the polyamine spermine. A BLAST search of protein databases revealed that PDPr is distantly related to the mitochondrial flavoprotein dimethylglycine dehydrogenase, which functions in choline degradation.^[6]

Function[edit]

The mitochondrial pyruvate dehydrogenase complex (PDC) catalyzes the oxidative decarboxylation of pyruvate, linking glycolysis to the tricarboxylic acid cycle and fatty acid (FA) synthesis. Knowledge of the mechanisms that regulate PDC activity is important, because PDC inactivation is crucial for glucose conservation when glucose is scarce, whereas adequate PDC activity is required to allow both ATP and FA production from glucose. The mechanisms that control mammalian PDC activity include its phosphorylation (inactivation) by a family of pyruvate dehydrogenase kinases (PDKs 1–4) and its dephosphorylation (activation, reactivation) by the pyruvate dehydrogenase phosphatases (PDPs 1 and 2).^[7]

Clinical significance[edit]

As PDPR is involved in the regulation of the central metabolic pathway, its participation in disease pathophysiology is likely, but there has been no published research on this thus far.^[5]

References[edit]

Further reading[edit]