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In [[biochemistry]], '''glucuronosyltransferase''', also called UDP-glucuronosyltransferase, is "a family of enzymes accepting a wide range of substrates, including phenols, alcohols, amines, and fatty acids. They function as drug-metabolizing enzymes that catalyze the conjugation of [[UDPglucuronic acid]] to a variety of endogenous and exogenous compounds."<ref>{{MeSH}}</ref> | In [[biochemistry]], '''glucuronosyltransferase''', also called UDP-glucuronosyltransferase, is "a family of enzymes accepting a wide range of substrates, including phenols, alcohols, amines, and fatty acids. They function as drug-metabolizing enzymes that catalyze the conjugation of [[UDPglucuronic acid]] to a variety of endogenous and exogenous compounds."<ref>{{MeSH}}</ref> | ||
Mutation in the UDP-glycuronosyltransferase gene cause [[Gilbert Syndrome]]<ref>{{OMIM|143500}}</ref> and [[Crigler-Najjar Syndrome]] types I<ref>{{OMIM|218800}}</ref> and II<ref>{{OMIM|606785}}</ref>. | |||
[[Anti-liver kidney microsome]] Type 3 (LKM3) [[autoantibody|autoantibodies]] may be present in chonic hepatitis D,<ref name="pmid8905121">{{cite journal| author=Obermayer-Straub P, Manns MP| title=Cytochromes P450 and UDP-glucuronosyl-transferases as hepatocellular autoantigens. | journal=Baillieres Clin Gastroenterol | year= 1996 | volume= 10 | issue= 3 | pages= 501-32 | pmid=8905121 | |||
| url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=clinical.uthscsa.edu/cite&retmode=ref&cmd=prlinks&id=8905121 }} </ref> [[autoimmune hepatitis]] and [[chronic active hepatitis]].<ref name="pmid14871643">{{cite journal| author=Fabien N, Desbos A, Bienvenu J, Magdalou J| title=Autoantibodies directed against the UDP-glucuronosyltransferases in human autoimmune hepatitis. | journal=Autoimmun Rev | year= 2004 | volume= 3 | issue= 1 | pages= 1-9 | pmid=14871643 | |||
| url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=clinical.uthscsa.edu/cite&retmode=ref&cmd=prlinks&id=14871643 | doi=10.1016/S1568-9972(03)00051-X }} </ref> | |||
Glucuronosyltransferase is part of the phase II drug metabolism of [[morphine]] and [[acetaminophen]].<ref name="pmid10427468">{{cite journal| author=de Wildt SN, Kearns GL, Leeder JS, van den Anker JN| title=Glucuronidation in humans. Pharmacogenetic and developmental aspects. | journal=Clin Pharmacokinet | year= 1999 | volume= 36 | issue= 6 | pages= 439-52 | pmid=10427468 | |||
| url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=clinical.uthscsa.edu/cite&retmode=ref&cmd=prlinks&id=10427468 }} </ref> | |||
Some drug interactions may be due to glucuronosyltransferase.<ref name="pmid15781124">{{cite journal| author=Kiang TK, Ensom MH, Chang TK| title=UDP-glucuronosyltransferases and clinical drug-drug interactions. | journal=Pharmacol Ther | year= 2005 | volume= 106 | issue= 1 | pages= 97-132 | pmid=15781124 | |||
| url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=clinical.uthscsa.edu/cite&retmode=ref&cmd=prlinks&id=15781124 | doi=10.1016/j.pharmthera.2004.10.013 }} </ref> | |||
==References== | ==References== | ||
<references/> | <references/> | ||
Latest revision as of 05:00, 12 April 2010
In biochemistry, glucuronosyltransferase, also called UDP-glucuronosyltransferase, is "a family of enzymes accepting a wide range of substrates, including phenols, alcohols, amines, and fatty acids. They function as drug-metabolizing enzymes that catalyze the conjugation of UDPglucuronic acid to a variety of endogenous and exogenous compounds."[1]
Mutation in the UDP-glycuronosyltransferase gene cause Gilbert Syndrome[2] and Crigler-Najjar Syndrome types I[3] and II[4].
Anti-liver kidney microsome Type 3 (LKM3) autoantibodies may be present in chonic hepatitis D,[5] autoimmune hepatitis and chronic active hepatitis.[6]
Glucuronosyltransferase is part of the phase II drug metabolism of morphine and acetaminophen.[7]
Some drug interactions may be due to glucuronosyltransferase.[8]
References
- ↑ Anonymous (2024), Glucuronosyltransferase (English). Medical Subject Headings. U.S. National Library of Medicine.
- ↑ Online Mendelian Inheritance in Man, OMIM®. Johns Hopkins University, Baltimore, MD. MIM Number: 143500. World Wide Web URL: http://omim.org/.
- ↑ Online Mendelian Inheritance in Man, OMIM®. Johns Hopkins University, Baltimore, MD. MIM Number: 218800. World Wide Web URL: http://omim.org/.
- ↑ Online Mendelian Inheritance in Man, OMIM®. Johns Hopkins University, Baltimore, MD. MIM Number: 606785. World Wide Web URL: http://omim.org/.
- ↑ Obermayer-Straub P, Manns MP (1996). "Cytochromes P450 and UDP-glucuronosyl-transferases as hepatocellular autoantigens.". Baillieres Clin Gastroenterol 10 (3): 501-32. PMID 8905121.
- ↑ Fabien N, Desbos A, Bienvenu J, Magdalou J (2004). "Autoantibodies directed against the UDP-glucuronosyltransferases in human autoimmune hepatitis.". Autoimmun Rev 3 (1): 1-9. DOI:10.1016/S1568-9972(03)00051-X. PMID 14871643. Research Blogging.
- ↑ de Wildt SN, Kearns GL, Leeder JS, van den Anker JN (1999). "Glucuronidation in humans. Pharmacogenetic and developmental aspects.". Clin Pharmacokinet 36 (6): 439-52. PMID 10427468.
- ↑ Kiang TK, Ensom MH, Chang TK (2005). "UDP-glucuronosyltransferases and clinical drug-drug interactions.". Pharmacol Ther 106 (1): 97-132. DOI:10.1016/j.pharmthera.2004.10.013. PMID 15781124. Research Blogging.