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{{enzyme
| Name = IMP dehydrogenase
| EC_number = 1.1.1.205
| CAS_number = 9028-93-7
| IUBMB_EC_number = 1/1/1/205
| GO_code = 0003938
| image = PDB 1meh EBI.jpg
| width =
| caption = Structure of IMPDH<ref name="pmid12559919">{{cite journal |author=Prosise GL, Luecke H |title=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 |journal=J. Mol. Biol. |volume=326 |issue=2 |pages=517–27 |date=February 2003 |pmid=12559919 |doi= 10.1016/S0022-2836(02)01383-9|url=}}</ref>
}}

'''IMP dehydrogenase''' {{EC number|1.1.1.205}} (Inosine-5'-monophosphate dehydrogenase) (Inosinic acid dehydrogenaseis) (IMPDH) an [[enzyme]] that converts [[inosine monophosphate]] to [[xanthosine monophosphate]]:<ref name="pmid13428767">{{cite journal | author = Magasanik B, Moyed HS, Gehring LB | title = Enzymes essential for the biosynthesis of nucleic acid guanine; inosine 5'-phosphate dehydrogenase of ''Aerobacter aerogenes'' | journal = J. Biol. Chem. | volume = 226 | issue = 1 | pages = 339–50 |date=May 1957 | pmid = 13428767 | doi = | url = | issn = }}</ref><ref name="pmid13778733">{{cite journal | author = Turner JF, King JE | title = Inosine 5'-phosphate dehydrogenase of pea seeds | journal = Biochem. J. | volume = 79 | issue = | pages = 147–51 |date=April 1961 | pmid = 13778733 | pmc = 1205560 | doi = | url = | issn = }}</ref><ref name="pmid19480389">{{cite journal | author = Hedstrom L | title = IMP dehydrogenase: structure, mechanism, and inhibition | journal = Chem. Rev. | volume = 109 | issue = 7 | pages = 2903–28 |date=July 2009 | pmid = 19480389 | doi = 10.1021/cr900021w | url = | issn = | pmc = 2737513 }}</ref><ref name="pmid18990827">{{cite journal | author = Pimkin M, Markham GD | title = Inosine 5'-monophosphate dehydrogenase | journal = Adv. Enzymol. Relat. Areas Mol. Biol. | volume = 76 | issue = | pages = 1–53 | year = 2009 | pmid = 18990827 | doi = | url = | issn = }}</ref>

:[[inosine monophosphate|inosine 5'-phosphate]] + [[nicotinamide adenine dinucleotide|NAD+]] + [[water|H2O]] <math>\rightleftharpoons</math> [[xanthosine monophosphate|xanthosine 5'-phosphate]] + NADH + H+

It [[Catalysis|catalyzes]] the rate-limiting reaction of ''[[De novo synthesis|de novo]]'' [[Guanosine triphosphate|GTP]] [[biosynthesis]].<ref name="pmid2902093">{{cite journal | author = Collart FR, Huberman E | title = Cloning and sequence analysis of the human and Chinese hamster inosine-5'-monophosphate dehydrogenase cDNAs | journal = J. Biol. Chem. | volume = 263 | issue = 30 | pages = 15769–72 |date=October 1988 | pmid = 2902093 | doi = | url = }}</ref>

IMP dehydrogenase is associated with [[Cell growth|cell proliferation]] and is a possible target for [[cancer]] [[chemotherapy]]. [[Mammalia]]n and [[bacteria]]l IMPDHs are [[tetramer]]s of identical [[polymer|chain]]s. There are two IMP dehydrogenase [[isozymes]] in [[Homo sapiens|human]]s.<ref name="pmid1969416">{{cite journal | author = Natsumeda Y, Ohno S, Kawasaki H, Konno Y, Weber G, Suzuki K | title = Two distinct cDNAs for human IMP dehydrogenase | journal = J. Biol. Chem. | volume = 265 | issue = 9 | pages = 5292–5 |date=March 1990 | pmid = 1969416 | doi = | url = }}</ref> IMP dehydrogenase nearly always contains a long insertion that has two [[CBS domain]]s within it.

The structure of this enzyme is composed of a [[TIM barrel]] domain with two [[CBS domain]]s inserted within a loop.<ref name="pmid12559919"/><ref name="pmid19480389"/>

It is inhibited by [[Mycophenolic acid]] [[ribavirin]], and 6TGMP (6-thioguanine monophosphate). 6TGMP inhibition prevents purine interconversion and thus the synthesis of purine nucleotides.

== Examples ==

Humans express the following two IMP dehydrogenase isozymes:
{|
|{{protein
|Name=[[IMPDH1|IMP dehydrogenase 1]]
|caption=
|image=
|width=
|HGNCid=6052
|Symbol=[[IMPDH1]]
|AltSymbols=RP10
|EntrezGene=3614
|OMIM=146690
|RefSeq=NM_000883
|UniProt=P20839
|PDB=
|ECnumber=1.1.1.205
|Chromosome=7
|Arm=q
|Band=31.3
|LocusSupplementaryData=-q32
}}
|{{protein
|Name=[[IMPDH2|IMP dehydrogenase 2]]
|caption=
|image=
|width=
|HGNCid=6053
|Symbol=[[IMPDH2]]
|AltSymbols= IMPD2
|EntrezGene=3615
|OMIM=146691
|RefSeq=NM_000884
|UniProt=P12268
|PDB=
|ECnumber=1.1.1.205
|Chromosome=3
|Arm=p
|Band=21.2
|LocusSupplementaryData=
}}
|}

==See also==
* [[Purine metabolism]]

==References==
{{reflist|1}}

== Further reading ==
{{refbegin}}
* {{cite journal | author = Wang J, Yang JW, Zeevi A, Webber SA, Girnita DM, Selby R, Fu J, Shah T, Pravica V, Hutchinson IV, Burckart GJ | title = IMPDH1 gene polymorphisms and association with acute rejection in renal transplant patients | journal = Clin. Pharmacol. Ther. | volume = 83 | issue = 5 | pages = 711–7 |date=May 2008 | pmid = 17851563 | doi = 10.1038/sj.clpt.6100347 | url = | issn = }}
{{refend}}

{{Alcohol oxidoreductases}}
{{Nucleotide metabolism}}

{{InterPro content|IPR001093}}

{{DEFAULTSORT:Imp Dehydrogenase}}
[[Category:EC 1.1.1]]
[[Category:NADH-dependent enzymes]]
[[Category:Enzymes of known structure]]

{{1.1.1-enzyme-stub}}

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