イノシン一リン酸デヒドロゲナーゼ、イノシン酸デヒドロゲナーゼ、イノシン酸脱水素酵素
WordNet
- the 9th letter of the Roman alphabet (同)i
- one who is playfully mischievous (同)scamp, monkey, rascal, rapscallion, scalawag, scallywag
PrepTutorEJDIC
- 『私は』私が
- iodineの化学記号
- 小悪魔;悪魔の子 / わんばく
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/09/05 01:26:16」(JST)
[Wiki en表示]
| IMP dehydrogenase |
|
Structure of IMPDH[1]
|
| Identifiers |
| EC number |
1.1.1.205 |
| CAS number |
9028-93-7 |
| Databases |
| IntEnz |
IntEnz view |
| BRENDA |
BRENDA entry |
| ExPASy |
NiceZyme view |
| KEGG |
KEGG entry |
| MetaCyc |
metabolic pathway |
| PRIAM |
profile |
| PDB structures |
RCSB PDB PDBe PDBsum |
| Gene Ontology |
AmiGO / EGO |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
|
IMP dehydrogenase EC 1.1.1.205 (Inosine-5'-monophosphate dehydrogenase) (Inosinic acid dehydrogenaseis) (IMPDH) an enzyme that converts inosine monophosphate to xanthosine monophosphate:[2][3][4][5]
- inosine 5'-phosphate + NAD+ + H2O xanthosine 5'-phosphate + NADH + H+
It catalyzes the rate-limiting reaction of de novo GTP biosynthesis.[6]
IMP dehydrogenase is associated with cell proliferation and is a possible target for cancer chemotherapy. Mammalian and bacterial IMPDHs are tetramers of identical chains. There are two IMP dehydrogenase isozymes in humans.[7] IMP dehydrogenase nearly always contains a long insertion that has two CBS domains within it.
The structure of this enzyme is composed of a TIM barrel domain with two CBS domains inserted within a loop.[1][4]
It is inhibited by Mycophenolic acid, ribavirin, and 6TGMP (6-thioguanine monophosphate). 6TGMP inhibition prevents purine interconversion and thus the synthesis of purine nucleotides.
Contents
- 1 Examples
- 2 See also
- 3 References
- 4 Further reading
Examples
Humans express the following two IMP dehydrogenase isozymes:
| IMP dehydrogenase 1 |
| Identifiers |
| Symbol |
IMPDH1 |
| Alt. symbols |
RP10 |
| Entrez |
3614 |
| HUGO |
6052 |
| OMIM |
146690 |
| RefSeq |
NM_000883 |
| UniProt |
P20839 |
| Other data |
| Locus |
Chr. 7 q31.3-q32 |
|
| IMP dehydrogenase 2 |
| Identifiers |
| Symbol |
IMPDH2 |
| Alt. symbols |
IMPD2 |
| Entrez |
3615 |
| HUGO |
6053 |
| OMIM |
146691 |
| RefSeq |
NM_000884 |
| UniProt |
P12268 |
| Other data |
| Locus |
Chr. 3 p21.2 |
|
See also
References
- ^ a b Prosise GL, Luecke H (February 2003). "Crystal structures of Tritrichomonasfoetus inosine monophosphate dehydrogenase in complex with substrate, cofactor and analogs: a structural basis for the random-in ordered-out kinetic mechanism". J. Mol. Biol. 326 (2): 517–27. doi:10.1016/S0022-2836(02)01383-9. PMID 12559919.
- ^ Magasanik B, Moyed HS, Gehring LB (May 1957). "Enzymes essential for the biosynthesis of nucleic acid guanine; inosine 5'-phosphate dehydrogenase of Aerobacter aerogenes". J. Biol. Chem. 226 (1): 339–50. PMID 13428767.
- ^ Turner JF, King JE (April 1961). "Inosine 5'-phosphate dehydrogenase of pea seeds". Biochem. J. 79: 147–51. PMC 1205560. PMID 13778733.
- ^ a b Hedstrom L (July 2009). "IMP dehydrogenase: structure, mechanism, and inhibition". Chem. Rev. 109 (7): 2903–28. doi:10.1021/cr900021w. PMC 2737513. PMID 19480389.
- ^ Pimkin M, Markham GD (2009). "Inosine 5'-monophosphate dehydrogenase". Adv. Enzymol. Relat. Areas Mol. Biol. 76: 1–53. PMID 18990827.
- ^ Collart FR, Huberman E (October 1988). "Cloning and sequence analysis of the human and Chinese hamster inosine-5'-monophosphate dehydrogenase cDNAs". J. Biol. Chem. 263 (30): 15769–72. PMID 2902093.
- ^ Natsumeda Y, Ohno S, Kawasaki H, Konno Y, Weber G, Suzuki K (March 1990). "Two distinct cDNAs for human IMP dehydrogenase". J. Biol. Chem. 265 (9): 5292–5. PMID 1969416.
Further reading
- Wang J, Yang JW, Zeevi A, Webber SA, Girnita DM, Selby R, Fu J, Shah T, Pravica V, Hutchinson IV, Burckart GJ (May 2008). "IMPDH1 gene polymorphisms and association with acute rejection in renal transplant patients". Clin. Pharmacol. Ther. 83 (5): 711–7. doi:10.1038/sj.clpt.6100347. PMID 17851563.
|
Oxidoreductases: alcohol oxidoreductases (EC 1.1)
|
|
| 1.1.1: NAD/NADP acceptor |
- 3-hydroxyacyl-CoA dehydrogenase
- 3-hydroxybutyryl-CoA dehydrogenase
- Alcohol dehydrogenase
- Aldo-keto reductase
- 1A1
- 1B1
- 1B10
- 1C1
- 1C3
- 1C4
- 7A2
- Aldose reductase
- Beta-Ketoacyl ACP reductase
- Carbohydrate dehydrogenases
- Carnitine dehydrogenase
- D-malate dehydrogenase (decarboxylating)
- DXP reductoisomerase
- Glucose-6-phosphate dehydrogenase
- Glycerol-3-phosphate dehydrogenase
- HMG-CoA reductase
- IMP dehydrogenase
- Isocitrate dehydrogenase
- Lactate dehydrogenase
- L-threonine dehydrogenase
- L-xylulose reductase
- Malate dehydrogenase
- Malate dehydrogenase (decarboxylating)
- Malate dehydrogenase (NADP+)
- Malate dehydrogenase (oxaloacetate-decarboxylating)
- Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
- Phosphogluconate dehydrogenase
- Sorbitol dehydrogenase
- Hydroxysteroid dehydrogenase: 3 Beta
- 11 Beta
- 17 Beta
|
|
| 1.1.2: cytochrome acceptor |
- D-lactate dehydrogenase (cytochrome)
- D-lactate dehydrogenase (cytochrome c-553)
- Mannitol dehydrogenase (cytochrome)
|
|
| 1.1.3: oxygen acceptor |
- Glucose oxidase
- L-gulonolactone oxidase
- Xanthine oxidase
|
|
| 1.1.4: disulfide as acceptor |
- Vitamin K epoxide reductase
- Vitamin-K-epoxide reductase (warfarin-insensitive)
|
|
| 1.1.5: quinone/similar acceptor |
- Malate dehydrogenase (quinone)
- Quinoprotein glucose dehydrogenase
|
|
| 1.1.99: other acceptors |
- Choline dehydrogenase
- L2HGDH
|
|
- 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: amino acid metabolism
- nucleotide enzymes
|
|
| Purine metabolism |
| Anabolism |
| R5P→IMP: |
- Ribose-phosphate diphosphokinase
- Amidophosphoribosyltransferase
- Phosphoribosylglycinamide formyltransferase
- AIR synthetase (FGAM cyclase)
- Phosphoribosylaminoimidazole carboxylase
- Phosphoribosylaminoimidazolesuccinocarboxamide synthase
- IMP synthase
|
|
| IMP→AMP: |
- Adenylosuccinate synthase
- Adenylosuccinate lyase
- reverse
|
|
| IMP→GMP: |
- IMP dehydrogenase
- GMP synthase
- reverse
|
|
|
| Nucleotide salvage |
- Hypoxanthine-guanine phosphoribosyltransferase
- Adenine phosphoribosyltransferase
|
|
| Catabolism |
- Adenosine deaminase
- Purine nucleoside phosphorylase
- Guanine deaminase
- Xanthine oxidase
- Urate oxidase
|
|
|
| Pyrimidine metabolism |
| Anabolism |
- CAD
- Carbamoyl phosphate synthase II
- Aspartate carbamoyltransferase
- Dihydroorotase
|
|
- Dihydroorotate dehydrogenase
- Orotidine 5'-phosphate decarboxylase/Uridine monophosphate synthetase
|
|
|
|
|
|
| Catabolism |
- Dihydropyrimidine dehydrogenase
- Dihydropyrimidinase/DPYS
- Beta-ureidopropionase/UPB1
|
|
|
| Deoxyribonucleotides |
- Ribonucleotide reductase
- Nucleoside-diphosphate kinase
- DCMP deaminase
- Thymidylate synthase
- Dihydrofolate reductase
|
|
|
|
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)
|
|
|
|
This article incorporates text from the public domain Pfam and InterPro IPR001093
UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
English Journal
- Autophagy suppression sensitizes glioma cells to IMP dehydrogenase inhibition-induced apoptotic death.
- Isakovic AM1, Dulovic M1, Markovic I1, Kravic-Stevovic T2, Bumbasirevic V2, Trajkovic V3, Isakovic A4.
- Experimental cell research.Exp Cell Res.2016 Nov 4. pii: S0014-4827(16)30363-9. doi: 10.1016/j.yexcr.2016.11.001. [Epub ahead of print]
- We investigated the role of autophagy, a process of controlled self-digestion, in the in vitro anticancer action of the inosine monophosphate dehydrogenase (IMPDH) inhibitor ribavirin. Ribavirin-triggered oxidative stress, caspase activation, and apoptotic death in U251 human glioma cells were assoc
- PMID 27818246
- Substrate and Cofactor Dynamics on Guanosine Monophosphate Reductase Probed by High Resolution Field Cycling 31P NMR Relaxometry.
- Rosenberg MM1, Redfield AG2, Roberts MF3, Hedstrom L4,5.
- The Journal of biological chemistry.J Biol Chem.2016 Oct 28;291(44):22988-22998. Epub 2016 Sep 9.
- Guanosine-5'-monophosphate reductase (GMPR) catalyzes the reduction of GMP to IMP and ammonia with concomitant oxidation of NADPH. Here we investigated the structure and dynamics of enzyme-bound substrates and cofactors by measuring 31P relaxation rates over a large magnetic field range using high r
- PMID 27613871
- Essential but not vulnerable: indazole sulfonamides targeting inosine monophosphate dehydrogenase as potential leads against Mycobacterium tuberculosis.
- Park Y, Pacitto A, Bayliss T, Cleghorn LA, Wang Z, Hartman T, Arora K, Ioerger TR, Sacchettini J, Rizzi M, Donini S, Blundell TL, Ascher DB, Rhee KY, Breda A, Zhou N, Dartois V, Jonnala SR, Via LE, Mizrahi V, Epemolu O, Stojanovski L, Simeons FR, Osuna-Cabello M, Ellis L, MacKenzie CJ, Smith AR, Davis SH, Murugesan D, Buchanan KI, Turner PA, Huggett M, Zuccotto F, Rebollo-Lopez MJ, Lafuente-Monasterio MJ, Sanz O, Santos Diaz G, Lelièvre J, Ballell L, Selenski C, Axtman M, Ghidelli-Disse S, Pflaumer H, Boesche M, Drewes G, Freiberg G, Kurnick MD, Srikumaran M, Kempf DJ, Green SR, Ray PC, Read KD, Wyatt PG, Barry Rd CE, Boshoff HI.
- ACS infectious diseases.ACS Infect Dis.2016 Oct 5. [Epub ahead of print]
- A potent, non-cytotoxic indazole sulfonamide was identified by high-throughput screening of >100,000 synthetic compounds for activity against Mycobacterium tuberculosis (Mtb). This non-cytotoxic compound did not directly inhibit cell wall biogenesis but triggered a slow lysis of Mtb cells as meas
- PMID 27704782
Japanese Journal
- 汎用性殺虫剤を投与したウィスター系雄ラットにおける血漿，赤血球膜結合酵素および細胞組織の変化
- , ,
- Journal of Pesticide Science advpub(0), 2015
- … Low doses (one-fourth of the LD50) of dichlorvos (DDVP), lambda-cyhalothrin (LMB), cypermethrin (CPM), and imidacloprid (IMP) were administered to adult male Wistar rats for 3 weeks. … Glucose-6-phosphate dehydrogenase (G6PD), glutathione-S-transferase (GST), acetylcholine (ACH), and body weight decreased significantly in DDVP- and LMB-treated rats only. … However, glutathione (GSH) levels decreased significantly in rats treated with DDVP and IMP. …
- NAID 130004939773
- 汎用殺虫剤を投与したウィスター系雄ラットにおける血漿，赤血球膜結合酵素および細胞組織の変化
- , ,
- Journal of Pesticide Science 40(1), 13-18, 2015
- … Low doses (one-fourth of the LD50) of dichlorvos (DDVP), lambda-cyhalothrin (LMB), cypermethrin (CPM), and imidacloprid (IMP) were administered to adult male Wistar rats for 3 weeks. … Glucose-6-phosphate dehydrogenase (G6PD), glutathione-S-transferase (GST), acetylcholine (ACH), and body weight decreased significantly in DDVP- and LMB-treated rats only. … However, glutathione (GSH) levels decreased significantly in rats treated with DDVP and IMP. …
- NAID 130004939752
- Signature-tagged mutagenesis of Vibrio vulnificus
- , , , , , , , , , , ,
- Journal of Veterinary Medical Science advpub(0), 2015
- … Transposon-inserted genes in the 11 attenuated mutants were those for IMP dehydrogenase, UDP-N-acetylglucosamine-2-epimerase, aspartokinase, phosphoribosylformylglycinamidine cyclo-ligase, malate Na (+) symporter and hypothetical protein. … When mice were immunized with an attenuated mutant strain into which IMP dehydrogenase had been inserted with a transposon, they were protected against V. …
- NAID 130004781124
Related Links
- IMP dehydrogenase. Alternative Name(s) IMP oxidoreductase. Inosinate dehydrogenase. Inosine 5'-monophosphate dehydrogenase. Inosine monophosphate oxidoreductase. Inosinic acid dehydrogenase. Reaction catalysed + + ...
- forum Join the Word of the Day Mailing List For webmasters TheFreeDictionary Google Bing? Word / Article Starts with Ends with Text ... Assignment of the human type I IMP dehydrogenase gene (IMPDH1) to chromosome 7831. ...
★リンクテーブル★
[★]
- 英
- IMP dehydrogenase
- 関
- イノシン一リン酸デヒドロゲナーゼ、イノシン酸デヒドロゲナーゼ
[★]
- 英
- IMP dehydrogenase
- 関
- イノシン一リン酸デヒドロゲナーゼ、イノシン酸脱水素酵素
[★]
- 英
- IMP dehydrogenase
- 関
- イノシン酸デヒドロゲナーゼ、イノシン酸脱水素酵素
[★]
[★]
[★]
[★]
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