From Wikipedia, the free encyclopedia
PDPR
Identifiers
Aliases PDPR, PDP3, pyruvate dehydrogenase phosphatase regulatory subunit
External IDs OMIM: 617835; MGI: 2442188; HomoloGene: 9948; GeneCards: PDPR; OMA: PDPR - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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
View/Edit Human View/Edit Mouse

Pyruvate dehydrogenase phosphatase regulatory subunit is a protein that in humans is encoded by the PDPR gene. [5]

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. [6]

Function

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

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

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000090857Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000033624Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: Pyruvate dehydrogenase phosphatase regulatory subunit".
  6. ^ Lawson JE, Park SH, Mattison AR, Yan J, Reed LJ (December 1997). "Cloning, expression, and properties of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase". The Journal of Biological Chemistry. 272 (50): 31625–9. doi: 10.1074/jbc.272.50.31625. PMID  9395502.
  7. ^ Sugden MC, Holness MJ (May 2003). "Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs". American Journal of Physiology. Endocrinology and Metabolism. 284 (5): E855-62. doi: 10.1152/ajpendo.00526.2002. PMID  12676647.

Further reading


From Wikipedia, the free encyclopedia
PDPR
Identifiers
Aliases PDPR, PDP3, pyruvate dehydrogenase phosphatase regulatory subunit
External IDs OMIM: 617835; MGI: 2442188; HomoloGene: 9948; GeneCards: PDPR; OMA: PDPR - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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
View/Edit Human View/Edit Mouse

Pyruvate dehydrogenase phosphatase regulatory subunit is a protein that in humans is encoded by the PDPR gene. [5]

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. [6]

Function

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

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

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000090857Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000033624Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: Pyruvate dehydrogenase phosphatase regulatory subunit".
  6. ^ Lawson JE, Park SH, Mattison AR, Yan J, Reed LJ (December 1997). "Cloning, expression, and properties of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase". The Journal of Biological Chemistry. 272 (50): 31625–9. doi: 10.1074/jbc.272.50.31625. PMID  9395502.
  7. ^ Sugden MC, Holness MJ (May 2003). "Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs". American Journal of Physiology. Endocrinology and Metabolism. 284 (5): E855-62. doi: 10.1152/ajpendo.00526.2002. PMID  12676647.

Further reading



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