WordNet
- any of a group of enzymes that act as a catalyst in the hydrolysis of organic phosphates
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/07/27 01:25:17」(JST)
[Wiki en表示]
| Pyruvate dehyrogenase phosphatase catalytic subunit 1 |
| Identifiers |
| Symbols |
PDP1; PDH; PDP; PDPC; PPM2C |
| External IDs |
OMIM: 605993 MGI: 2685870 HomoloGene: 31928 GeneCards: PDP1 Gene |
| EC number |
3.1.3.43 |
| Gene Ontology |
| Molecular function |
• protein serine/threonine phosphatase activity
• [pyruvate dehydrogenase (lipoamide) phosphatase activity]
• metal ion binding
|
| Cellular component |
• mitochondrial matrix
|
| Biological process |
• pyruvate metabolic process
• regulation of acetyl-CoA biosynthetic process from pyruvate
• peptidyl-threonine dephosphorylation
• small molecule metabolic process
|
| Sources: Amigo / QuickGO |
|
| 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 |
[1] |
[2] |
|
|
|
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.
Contents
- 1 Function
- 2 Clinical significance
- 3 References
- 4 Further reading
- 5 External links
Function[edit]
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[edit]
Mutation in this gene causes pyruvate dehydrogenase phosphatase deficiency.[1]
References[edit]
- ^ a b c "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[edit]
- 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[edit]
- 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.
|
Hydrolase: esterases (EC 3.1)
|
|
| 3.1.1: Carboxylic ester hydrolases |
- Cholinesterase
- Acetylcholinesterase
- Butyrylcholinesterase
- Pectinesterase
- 6-phosphogluconolactonase
- PAF acetylhydrolase
- Lipase
- Bile salt-dependent
- Gastric/Lingual
- Pancreatic
- Lysosomal
- Hormone-sensitive
- Endothelial
- Hepatic
- Lipoprotein
- Monoacylglycerol
- Diacylglycerol
|
|
| 3.1.2: Thioesterase |
- Palmitoyl protein thioesterase
- Ubiquitin carboxy-terminal hydrolase L1
|
|
| 3.1.3: Phosphatase |
- Alkaline phosphatase
- Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases
- Nucleotidase
- Glucose 6-phosphatase
- Fructose 1,6-bisphosphatase
- Phosphoprotein phosphatase
- OCRL
- Pyruvate dehydrogenase phosphatase
- Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
- PTEN
- Phytase
- Inositol-phosphate phosphatase
- Phosphoprotein phosphatase: Protein tyrosine phosphatase
- Protein serine/threonine phosphatase
- Dual-specificity phosphatase
|
|
| 3.1.4: Phosphodiesterase |
- Autotaxin
- Phospholipase
- Sphingomyelin phosphodiesterase
- PDE1
- PDE2
- PDE3
- PDE4A/PDE4B
- PDE5
- Lecithinase (Clostridium perfringens alpha toxin)
- Cyclic nucleotide phosphodiesterase
|
|
| 3.1.6: Sulfatase |
- arylsulfatase
- Arylsulfatase A
- Arylsulfatase B
- Arylsulfatase E
- Steroid sulfatase
- Galactosamine-6 sulfatase
- Iduronate-2-sulfatase
- N-acetylglucosamine-6-sulfatase
|
|
Nuclease (includes
deoxyribonuclease and
ribonuclease) |
| 3.1.11-16: Exonuclease |
| Exodeoxyribonuclease |
|
|
| Exoribonuclease |
|
|
|
| 3.1.21-31: Endonuclease |
| Endodeoxyribonuclease |
- Deoxyribonuclease I
- Deoxyribonuclease II
- Deoxyribonuclease IV
- Restriction enzyme
- UvrABC endonuclease
|
|
| Endoribonuclease |
- RNase III
- RNase H
- RNase P
- RNase A
- RNase T1
- RNA-induced silencing complex
|
|
| either deoxy- or ribo- |
- Aspergillus nuclease S1
- Micrococcal nuclease
|
|
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
|
Metabolism: Citric acid cycle enzymes
|
|
| Cycle |
- Citrate synthase
- Aconitase
- Isocitrate dehydrogenase
- Oxoglutarate dehydrogenase
- Succinyl CoA synthetase
- Succinate dehydrogenase (SDHA)
- Fumarase
- Malate dehydrogenase and ETC
|
|
| Anaplerotic |
|
to acetyl-CoA
|
- Pyruvate dehydrogenase complex (E1, E2, E3)
- (regulated by Pyruvate dehydrogenase kinase and Pyruvate dehydrogenase phosphatase)
|
|
|
to α-ketoglutaric acid
|
|
|
|
to succinyl-CoA
|
|
|
|
to oxaloacetate
|
- Pyruvate carboxylase
- Aspartate transaminase
|
|
|
Mitochondrial
electron transport chain/
oxidative phosphorylation |
|
Primary
|
- Complex I/NADH dehydrogenase
- Complex II/Succinate dehydrogenase
- Coenzyme Q
- Complex III/Coenzyme Q - cytochrome c reductase
- Cytochrome c
- Complex IV/Cytochrome c oxidase
- Coenzyme Q10 synthesis: COQ2
- COQ3
- COQ4
- COQ5
- COQ6
- COQ7
- COQ9
- COQ10A
- COQ10B
- PDSS1
- PDSS2
|
|
|
Other
|
- Alternative oxidase
- Electron-transferring-flavoprotein dehydrogenase
|
|
|
|
|
mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
|
k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
|
m (A16/C10), i (k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
|
|
|
|
UpToDate Contents
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English Journal
- Silencing gastrin-releasing peptide receptor suppresses key regulators of aerobic glycolysis in neuroblastoma cells.
- Rellinger EJ1, Romain C, Choi S, Qiao J, Chung DH.
- Pediatric blood & cancer.Pediatr Blood Cancer.2015 Apr;62(4):581-6. doi: 10.1002/pbc.25348. Epub 2015 Jan 28.
- BACKGROUND: Under normoxic conditions, cancer cells use aerobic glycolysis as opposed to glucose oxidation for energy production; this altered metabolism correlates with poor outcomes in neuroblastoma. Hypoxia-inducible factor-1 alpha (HIF-1α) and pyruvate dehydrogenase kinase 4 (PDK4) regulate aer
- PMID 25630799
- Exercise-induced regulation of key factors in substrate choice and gluconeogenesis in mouse liver.
- Knudsen JG1, Biensø RS, Hassing HA, Jakobsen AH, Pilegaard H.
- Molecular and cellular biochemistry.Mol Cell Biochem.2015 Feb 22. [Epub ahead of print]
- As the demand for hepatic glucose production increases during exercise, regulation of liver substrate choice and gluconeogenic activity becomes essential. The aim of the present study was to investigate the effect of a single exercise bout on gluconeogenic protein content and regulation of enzymes i
- PMID 25702176
- Insulin Priming Effect on Estradiol-induced Breast Cancer Metabolism and Growth.
- Wairagu PM1, Phan AN, Kim MK, Han J, Kim HW, Choi JW, Kim KW, Cha SK, Park KH, Jeong Y.
- Cancer biology & therapy.Cancer Biol Ther.2015 Feb 20:0. [Epub ahead of print]
- Diabetes is a risk factor for breast cancer development and is associated with poor prognosis for breast cancer patients. However, the molecular and biochemical mechanisms underlying the association between diabetes and breast cancer have not been fully elucidated. Here, we investigated estradiol re
- PMID 25701261
Japanese Journal
- Hormonal Regulation of Glycolytic Enzyme Gene and Pyruvate Dehydrogenase Kinase/Phosphatase Gene Transcription
- Antihyperglycemic Effect of Mangiferin in Streptozotocin Induced Diabetic Rats
- Hepatoprotective Nature of Seaweed Alcoholic Extract on Acetaminophen Induced Hepatic Oxidative Stress
Related Links
- Clinical Synopsis Phenotypic Series TEXT A number sign (#) is used with this entry because pyruvate dehydrogenase phosphatase deficiency can be caused by ...
- pyruvate dehydrogenase phosphatase 1, 2, PDP1, PDP2 Structure and Function: The pyruvate dehydrogenase complex (PDH) is at the centre of aerobic carbohydrate metabolism. It is localized in the matrix space of mitochondria ...
Related Pictures
★リンクテーブル★
[★]
- 英
- pyruvate dehydrogenase phosphatase
[★]
- 英
- pyruvate dehydrogenase phosphatase
[★]
ホスファターゼ、フォスファターゼ、脱リン酸化酵素、脱リン酸酵素
- 関
- phosphohydrolase、phosphoric monoester hydrolase
[★]
脱水素酵素 デヒドロゲナーゼ
[★]
脱水素酵素 デヒドロゲナーゼ
[★]
ピルビン酸デヒドロゲナーゼ
[★]
ピルビン酸 pyruvic acid