アデノシン一リン酸デアミナーゼ、アデニル酸デアミナーゼ、アデニル酸脱アミノ酵素、AMPデアミナーゼ
WordNet
- the 1st letter of the Roman alphabet (同)a
- the blood group whose red cells carry the A antigen (同)type_A, group A
PrepTutorEJDIC
- answer / ampere
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2014/07/14 23:54:46」(JST)
[Wiki en表示]
Adenosine monophosphate deaminase 1 |
Identifiers |
Symbols |
AMPD1 ; MAD; MADA |
External IDs |
OMIM: 102770 MGI: 88015 HomoloGene: 20 ChEMBL: 2869 GeneCards: AMPD1 Gene |
EC number |
3.5.4.6 |
Gene ontology |
Molecular function |
• AMP deaminase activity
• myosin heavy chain binding
• metal ion binding
|
Cellular component |
• cytosol
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Biological process |
• purine nucleobase metabolic process
• response to organic substance
• IMP salvage
• purine-containing compound salvage
• small molecule metabolic process
• nucleobase-containing small molecule metabolic process
|
Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
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Entrez |
270 |
229665 |
|
Ensembl |
ENSG00000116748 |
ENSMUSG00000070385 |
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UniProt |
P23109 |
Q3V1D3 |
|
RefSeq (mRNA) |
NM_000036 |
NM_001033303 |
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RefSeq (protein) |
NP_000027 |
NP_001028475 |
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Location (UCSC) |
Chr 1:
115.22 – 115.24 Mb |
Chr 3:
103.07 – 103.1 Mb |
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PubMed search |
[1] |
[2] |
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AMP deaminase 1 is an enzyme that in humans is encoded by the AMPD1 gene.[1][2]
Adenosine monophosphate deaminase is an enzyme that converts adenosine monophosphate (AMP) to inosine monophosphate (IMP), freeing an ammonia molecule in the process.
Contents
- 1 Function
- 2 Function
- 3 Pathology
- 4 References
- 5 Further reading
- 6 External links
Function
Adenosine monophosphate deaminase 1 catalyzes the deamination of AMP to IMP in skeletal muscle and plays an important role in the purine nucleotide cycle. Two other genes have been identified, AMPD2 and AMPD3, for the liver- and erythrocyte-specific isoforms, respectively. Deficiency of the muscle-specific enzyme is apparently a common cause of exercise-induced myopathy and probably the most common cause of metabolic myopathy in the human.[2]
Function
It is a part of the metabolic process that converts sugar, fat, and protein into cellular energy.[citation needed]
In order to use energy, a cell converts one of the above fuels into adenosine triphosphate (ATP) via the mitochondria. Cellular processes, especially muscles, then convert the ATP into adenosine diphosphate (ADP), freeing the energy to do work.[citation needed]
A new research report shows that the widely-prescribed diabetes medication metformin works on AMP kinase by directly inhibiting AMP deaminase, thereby increasing cellular AMP.[3]
Pathology
A deficiency is associated with myoadenylate deaminase deficiency.
-
adenosine monophosphate (AMP)
-
inosine monophosphate (IMP)
References
- ^ Mahnke-Zizelman DK, Sabina RL (October 1992). "Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons". J. Biol. Chem. 267 (29): 20866–77. PMID 1400401.
- ^ a b EntrezGene 270
- ^ Ouyang J, Parakhia RA, Ochs RS (January 2011). "Metformin activates AMP kinase through inhibition of AMP deaminase". J. Biol. Chem. 286 (1): 1–11. doi:10.1074/jbc.M110.121806. PMC 3012963. PMID 21059655. [unreliable medical source?]
Further reading
- Fishbein WN, Armbrustmacher VW, Griffin JL (1978). "Myoadenylate deaminase deficiency: a new disease of muscle.". Science 200 (4341): 545–8. doi:10.1126/science.644316. PMID 644316.
- Sabina RL, Fishbein WN, Pezeshkpour G, et al. (1992). "Molecular analysis of the myoadenylate deaminase deficiencies.". Neurology 42 (1): 170–9. doi:10.1212/wnl.42.1.170. PMID 1370861.
- Morisaki T, Gross M, Morisaki H, et al. (1992). "Molecular basis of AMP deaminase deficiency in skeletal muscle.". Proc. Natl. Acad. Sci. U.S.A. 89 (14): 6457–61. doi:10.1073/pnas.89.14.6457. PMC 49520. PMID 1631143.
- Sabina RL, Morisaki T, Clarke P, et al. (1990). "Characterization of the human and rat myoadenylate deaminase genes.". J. Biol. Chem. 265 (16): 9423–33. PMID 2345176.
- Dale GL (1989). "Radioisotopic assay for erythrocyte adenosine 5'-monophosphate deaminase.". Clin. Chim. Acta 182 (1): 1–7. doi:10.1016/0009-8981(89)90144-7. PMID 2502331.
- Mercelis R, Martin JJ, Dehaene I, et al. (1981). "Myoadenylate deaminase deficiency in a patient with facial and limb girdle myopathy.". J. Neurol. 225 (3): 157–66. doi:10.1007/BF00313744. PMID 6167680.
- van Laarhoven JP, de Gast GC, Spierenburg GT, de Bruyn CH (1983). "Enzymological studies in chronic lymphocytic leukemia.". Leuk. Res. 7 (2): 261–7. doi:10.1016/0145-2126(83)90016-4. PMID 6406772.
- Kelemen J, Rice DR, Bradley WG, et al. (1982). "Familial myoadenylate deaminase deficiency and exertional myalgia.". Neurology 32 (8): 857–63. doi:10.1212/wnl.32.8.857. PMID 7201581.
- Baumeister FA, Gross M, Wagner DR, et al. (1993). "Myoadenylate deaminase deficiency with severe rhabdomyolysis.". Eur. J. Pediatr. 152 (6): 513–5. doi:10.1007/BF01955062. PMID 8335021.
- Morisaki T, Holmes EW (1993). "Functionally distinct elements are required for expression of the AMPD1 gene in myocytes.". Mol. Cell. Biol. 13 (9): 5854–60. PMC 360332. PMID 8355716.
- Bruno C, Minetti C, Shanske S, et al. (1998). "Combined defects of muscle phosphofructokinase and AMP deaminase in a child with myoglobinuria.". Neurology 50 (1): 296–8. doi:10.1212/wnl.50.1.296. PMID 9443500.
- Hisatome I, Morisaki T, Kamma H, et al. (1998). "Control of AMP deaminase 1 binding to myosin heavy chain.". Am. J. Physiol. 275 (3 Pt 1): C870–81. PMID 9730972.
- Sims B, Powers RE, Sabina RL, Theibert AB (1999). "Elevated adenosine monophosphate deaminase activity in Alzheimer's disease brain.". Neurobiol. Aging 19 (5): 385–91. doi:10.1016/S0197-4580(98)00083-9. PMID 9880040.
- Loh E, Rebbeck TR, Mahoney PD, et al. (1999). "Common variant in AMPD1 gene predicts improved clinical outcome in patients with heart failure.". Circulation 99 (11): 1422–5. doi:10.1161/01.cir.99.11.1422. PMID 10086964.
- Abe M, Higuchi I, Morisaki H, et al. (2000). "Myoadenylate deaminase deficiency with progressive muscle weakness and atrophy caused by new missense mutations in AMPD1 gene: case report in a Japanese patient.". Neuromuscul. Disord. 10 (7): 472–7. doi:10.1016/S0960-8966(00)00127-9. PMID 10996775.
- Morisaki H, Higuchi I, Abe M, et al. (2001). "First missense mutations (R388W and R425H) of AMPD1 accompanied with myopathy found in a Japanese patient.". Hum. Mutat. 16 (6): 467–72. doi:10.1002/1098-1004(200012)16:6<467::AID-HUMU3>3.0.CO;2-V. PMID 11102975.
- Gross M, Rötzer E, Kölle P, et al. (2002). "A G468-T AMPD1 mutant allele contributes to the high incidence of myoadenylate deaminase deficiency in the Caucasian population.". Neuromuscul. Disord. 12 (6): 558–65. doi:10.1016/S0960-8966(02)00008-1. PMID 12117480.
- Mahnke-Zizelman DK, Sabina RL (2003). "N-terminal sequence and distal histidine residues are responsible for pH-regulated cytoplasmic membrane binding of human AMP deaminase isoform E.". J. Biol. Chem. 277 (45): 42654–62. doi:10.1074/jbc.M203473200. PMID 12213808.
External links
- AMP Deaminase at the US National Library of Medicine Medical Subject Headings (MeSH)
Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
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3.5.1: Linear amides /
Amidohydrolases |
- Asparaginase
- Glutaminase
- Urease
- Biotinidase
- Aspartoacylase
- Ceramidase
- Aspartylglucosaminidase
- Fatty acid amide hydrolase
- Histone deacetylase
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3.5.2: Cyclic amides/
Amidohydrolases |
- Barbiturase
- Beta-lactamase
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3.5.3: Linear amidines/
Ureohydrolases |
- Arginase
- Agmatinase
- Protein-arginine deiminase
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3.5.4: Cyclic amidines/
Aminohydrolases |
- Guanine deaminase
- Adenosine deaminase
- AMP deaminase
- Inosine monophosphate synthase
- DCMP deaminase
- GTP cyclohydrolase I
- Cytidine deaminase
- AICDA
- Activation-Induced (Cytidine) Deaminase
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3.5.5: Nitriles/
Aminohydrolases |
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3.5.99: Other |
- Riboflavinase
- Thiaminase II
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- 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
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- Metabolism: amino acid metabolism
- nucleotide enzymes
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Purine metabolism |
Anabolism |
R5P→IMP: |
- Ribose-phosphate diphosphokinase
- Amidophosphoribosyltransferase
- Phosphoribosylglycinamide formyltransferase
- AIR synthetase (FGAM cyclase)
- Phosphoribosylaminoimidazole carboxylase
- Phosphoribosylaminoimidazolesuccinocarboxamide synthase
- IMP synthase
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IMP→AMP: |
- Adenylosuccinate synthase
- Adenylosuccinate lyase
- reverse
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IMP→GMP: |
- IMP dehydrogenase
- GMP synthase
- reverse
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Nucleotide salvage |
- Hypoxanthine-guanine phosphoribosyltransferase
- Adenine phosphoribosyltransferase
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Catabolism |
- Adenosine deaminase
- Purine nucleoside phosphorylase
- Guanine deaminase
- Xanthine oxidase
- Urate oxidase
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Pyrimidine metabolism |
Anabolism |
- CAD
- Carbamoyl phosphate synthase II
- Aspartate carbamoyltransferase
- Dihydroorotase
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- Dihydroorotate dehydrogenase
- Orotidine 5'-phosphate decarboxylase/Uridine monophosphate synthetase
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Catabolism |
- Dihydropyrimidine dehydrogenase
- Dihydropyrimidinase/DPYS
- Beta-ureidopropionase/UPB1
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Deoxyribonucleotides |
- Ribonucleotide reductase
- Nucleoside-diphosphate kinase
- DCMP deaminase
- Thymidylate synthase
- Dihydrofolate reductase
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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
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k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
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m (A16/C10), i (k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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UpToDate Contents
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English Journal
- Activities of ectonucleotidases and adenosine deaminase in platelets of dogs experimentally infected with Rangelia vitalii.
- Paim CB, Da Silva AS, Paim FC, França RT, Costa MM, Souza VC, Pimentel VC, Jaques JA, Mazzanti CM, Leal DB, Monteiro SG, Schetinger MR, Lopes ST.SourceDepartment of Small Animals, Universidade Federal de Santa Maria, Brazil.
- Experimental parasitology.Exp Parasitol.2012 Mar 27. [Epub ahead of print]
- Rangeliosis is a disease which affects dogs in Brazil, caused by a piroplasm known as Rangelia vitalii. This disease causes a lot of clinico-pathological features, including the coagulation disorders associated with bleeding. The cause of these changes has not yet been determined. Considering the as
- PMID 22475775
- Overexpression of AMP-metabolizing enzymes controls adenine nucleotide levels and AMPK activation in HEK293T cells.
- Plaideau C, Liu J, Hartleib-Geschwindner J, Bastin-Coyette L, Bontemps F, Oscarsson J, Hue L, Rider MH.Source*Université Catholique de Louvain and de Duve Institute, Brussels, Belgium; and.
- FASEB journal : official publication of the Federation of American Societies for Experimental Biology.FASEB J.2012 Mar 13. [Epub ahead of print]
- We investigated whether overexpression of AMP-metabolizing enzymes in intact cells would modulate oligomycin-induced AMPK activation. Human embryonic kidney (HEK) 293T cells were transiently transfected with increasing amounts of plasmid vectors to obtain a graded increase in overexpression of AMP-d
- PMID 22415305
Japanese Journal
- Uptake of AMP, ADP, and ATP in Escherichia coli W
- WATANABE Kimiko,TOMIOKA Satsuki,TANIMURA Kiyoko,OKU Hisae,ISOI Koichiro
- Bioscience, biotechnology, and biochemistry 75(1), 7-12, 2011-01-23
- … The uptake activity ratio for AMP, ADP, and ATP in mutant (T-1) cells of Escherichia coli W, deficient in de novo purine biosynthesis at a point between IMP and 5-aminoimidazole-4-carboxiamide-1-β-D-ribofuranoside (AICAR), was 1:0.43:0.19. … AMP > … About 2-fold more radioactive purine bases than purine nucleosides were detected in the cytoplasm after 5 min in an experiment with [8-14C]AMP and T-1 cells. …
- NAID 10027896383
- β_3-adrenoceptor-mediated increased circulating transaminase levels in mice treated with its agonist BRL 37344
- KASAHARA Hiroko,MUTO Shin-ichi,MOTOKAWA Yoshiyuki,ARISAKA Nobuhiko,KOBAYASHI Sayaka,SOUMA Shinji,KURODA Junji
- Journal of toxicological sciences 35(5), 779-784, 2010-10-01
- … The transaminase changes were not accompanied by increases in circulating levels of other hepatocellular enzymes, including guanine deaminase (GUA), glutamate dehydrogenase (GLDH), and lactate dehydrogenase (LDH), or any morphological hepatocellular injury. …
- NAID 10026669477
Related Links
- AMP-deaminase Adenyl deaminase EC Number EC 3.5.4.6 作用 5’-アデニン酸(5’-AMP)を加水分解して5’-イノシン酸(5’-IMP)とアンモニアを生成する酵素である。本酵素は、アデニル酸デアミナーゼ、アデニルデアミナーゼとも 用途 ...
- AMP deaminase. 0 likes · 0 talking about this. AMP deaminase 1 is an enzyme that in humans is encoded by the AMPD1 gene. ... Wikipedia Content from the Wikipedia article AMP deaminase (contributors) licensed under CC-BY ...
★リンクテーブル★
[★]
- 英
- AMP deaminase
- 関
- アデノシン一リン酸デアミナーゼ、AMPデアミナーゼ、アデニル酸脱アミノ酵素
[★]
- 英
- AMP deaminase
- 関
- アデノシン一リン酸デアミナーゼ、アデニル酸デアミナーゼ、AMPデアミナーゼ
[★]
- 英
- AMP deaminase
- 関
- アデニル酸デアミナーゼ、AMPデアミナーゼ、アデニル酸脱アミノ酵素
[★]
アデニル酸デアミナーゼ欠損症
[★]
[★]
[★]
アデノシン一リン酸 adenosine monophosphate adenosine 5'-monophosphate
[★]
デアミナーゼ、脱アミノ酵素