Pyruvate dehydrogenase phosphatase
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| Pyruvate dehyrogenase phosphatase catalytic subunit 1 | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | PDP1; PDH; PDP; PDPC; PPM2C | ||||||||||||
| External IDs | OMIM: 605993 MGI: 2685870 HomoloGene: 31928 GeneCards: PDP1 Gene | ||||||||||||
| EC number | 3.1.3.43 | ||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 54704 | 381511 | |||||||||||
| Ensembl | ENSG00000164951 | ENSMUSG00000049225 | |||||||||||
| UniProt | Q9P0J1 | Q3UV70 | |||||||||||
| RefSeq (mRNA) | NM_001161778 | NM_001033453 | |||||||||||
| RefSeq (protein) | NP_001155251 | NP_001028625 | |||||||||||
| Location (UCSC) | Chr 8: 94.87 – 94.94 Mb | Chr 4: 11.96 – 11.97 Mb | |||||||||||
| PubMed search | |||||||||||||
pyruvate dehyrogenase phosphatase catalytic subunit 1 (PDPC 1), also known as protein phosphatase 2C, is an enzyme that in humans is encoded by the PDP1gene.[1][2] PDPC 1 is an enzyme which serves to reverse the effects of pyruvate dehydrogenase kinase upon pyruvate dehydrogenase.
Function
Pyruvate dehydrogenase (E1) is one of the three components (E1, E2, and E3) of the large pyruvate dehydrogenase complex. Pyruvate dehydrogenase kinases catalyze phosphorylation of serine residues of E1 to inactivate the E1 component and inhibit the complex. Pyruvate dehydrogenase phosphatases catalyze the dephosphorylation and activation of the E1 component to reverse the effects of pyruvate dehydrogenase kinases. Pyruvate dehydrogenase phosphatase is a heterodimer consisting of catalytic and regulatory subunits. Two catalytic subunits have been reported; one is predominantly expressed in skeletal muscle and another one is much more abundant in the liver. The catalytic subunit, encoded by this gene, is the former, and belongs to the protein phosphatase 2C (PP2C) superfamily. Along with the pyruvate dehydrogenase complex and pyruvate dehydrogenase kinases, this enzyme is located in the mitochondrial matrix.[1]
Clinical significance
Mutation in this gene causes pyruvate dehydrogenase phosphatase deficiency.[1]
References
- ↑ 1.0 1.1 1.2 "Entrez Gene: pyruvate dehyrogenase phosphatase catalytic subunit 1".
- ↑ Lawson JE, Niu XD, Browning KS, Trong HL, Yan J, Reed LJ (September 1993). "Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C". Biochemistry 32 (35): 8987–93. doi:10.1021/bi00086a002. PMID 8396421.
Further reading
- Piccinini M, Mostert M, Alberto G et al. (2005). "Down-regulation of pyruvate dehydrogenase phosphatase in obese subjects is a defect that signals insulin resistance". Obes. Res. 13 (4): 678–86. doi:10.1038/oby.2005.76. PMID 15897476.
- Kimura K, Wakamatsu A, Suzuki Y et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
- Hu RM, Han ZG, Song HD et al. (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946.
- Auffray C, Behar G, Bois F et al. (1995). "[IMAGE: molecular integration of the analysis of the human genome and its expression]". C. R. Acad. Sci. III, Sci. Vie 318 (2): 263–72. PMID 7757816.
- Lejeune F, Li X, Maquat LE (2003). "Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities". Mol. Cell 12 (3): 675–687. doi:10.1016/S1097-2765(03)00349-6. PMID 14527413.
- Cameron JM, Maj M, Levandovskiy V et al. (2009). "Pyruvate dehydrogenase phosphatase 1 (PDP1) null mutation produces a lethal infantile phenotype". Hum. Genet. 125 (3): 319–26. doi:10.1007/s00439-009-0629-6. PMID 19184109.
- Maj MC, MacKay N, Levandovskiy V et al. (2005). "Pyruvate dehydrogenase phosphatase deficiency: identification of the first mutation in two brothers and restoration of activity by protein complementation". J. Clin. Endocrinol. Metab. 90 (7): 4101–7. doi:10.1210/jc.2005-0123. PMID 15855260.
- Sugden MC, Holness MJ (2003). "Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs". Am. J. Physiol. Endocrinol. Metab. 284 (5): E855–62. doi:10.1152/ajpendo.00526.2002. PMID 12676647.
- Kato J, Kato M (2010). "Crystallization and preliminary crystallographic studies of the catalytic subunits of human pyruvate dehydrogenase phosphatase isoforms 1 and 2". Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66 (Pt 3): 342–345. doi:10.1107/S1744309110003131. PMC 2833053. PMID 20208177.
- Korotchkina LG, Patel MS (1995). "Mutagenesis studies of the phosphorylation sites of recombinant human pyruvate dehydrogenase. Site-specific regulation". J. Biol. Chem. 270 (24): 14297–304. doi:10.1074/jbc.270.24.14297. PMID 7782287.
- Stellingwerff T, Spriet LL, Watt MJ et al. (2006). "Decreased PDH activation and glycogenolysis during exercise following fat adaptation with carbohydrate restoration". Am. J. Physiol. Endocrinol. Metab. 290 (2): E380–8. doi:10.1152/ajpendo.00268.2005. PMID 16188909.
- Ito M, Kobashi H, Naito E et al. (1992). "Decrease of pyruvate dehydrogenase phosphatase activity in patients with congenital lactic acidemia". Clin. Chim. Acta 209 (1–2): 1–7. doi:10.1016/0009-8981(92)90327-M. PMID 1327585.
- Adams MD, Kerlavage AR, Fleischmann RD et al. (1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence". Nature 377 (6547 Suppl): 3–174. PMID 7566098.
- Caruso M, Maitan MA, Bifulco G et al. (2001). "Activation and mitochondrial translocation of protein kinase Cdelta are necessary for insulin stimulation of pyruvate dehydrogenase complex activity in muscle and liver cells". J. Biol. Chem. 276 (48): 45088–97. doi:10.1074/jbc.M105451200. PMID 11577086.
- Gerhard DS, Wagner L, Feingold EA et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Bonaldo MF, Lennon G, Soares MB (1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Strausberg RL, Feingold EA, Grouse LH et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Huang B, Gudi R, Wu P et al. (1998). "Isoenzymes of pyruvate dehydrogenase phosphatase. DNA-derived amino acid sequences, expression, and regulation". J. Biol. Chem. 273 (28): 17680–8. doi:10.1074/jbc.273.28.17680. PMID 9651365.
External links
- Pyruvate Dehydrogenase Phosphatase at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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