PDPR

Also known as PDP3, pyruvate dehydrogenase phosphatase regulatory subunit

Pyruvate dehydrogenase phosphatase regulatory subunit is a protein that in humans is encoded by the PDPR gene.

Gene data

PDPR

Name: pyruvate dehydrogenase phosphatase regulatory subunit
Type: protein-coding
Aliases: PDP3

Pyruvate dehydrogenase complex (PDC) catalyzes the oxidative decarboxylation of pyruvate and links glycolysis to the tricarboxylic acid cycle and fatty acid synthesis. The dephosphorylation and reactivation of PDC is catalyzed by pyruvate dehydrogenase phosphatase (PDP). The dimeric PDP has a catalytic subunit and a regulatory subunit. This gene encodes the FAD-containing regulatory subunit of PDP. The encoded protein acts to decrease the sensitivity of the PDP catalytic subunit to magnesium ions. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jan 2017].

via MyGene.info

Gene · Ensembl

pyruvate dehydrogenase phosphatase regulatory subunit

Symbol: PDPR
Biotype: Protein coding
Organism: Homo sapiens
Location: 16:70,114,225-70,162,537
Strand: Forward (+)
Assembly: GRCh38

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via Ensembl · EMBL-EBI

Wikidata facts

Show 5 more facts

HomoloGene ID: 9948
exact match: identifiers.org/ncbigene/55066
genomic end: 70162537
genomic start: 70114332
cytogenetic location: 16q22.1

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via Wikidata · CC0

~2 min read

Article

5 sections

Contents

Structure
Function
Clinical significance
References
Further reading

Pyruvate dehydrogenase phosphatase regulatory subunit is a protein that in humans is encoded by the PDPR gene.

==Structure== 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.