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Article: Catalytic characteristics of CYP3A22-dependent mequindox detoxification

TitleCatalytic characteristics of CYP3A22-dependent mequindox detoxification
Authors
KeywordsCarbonyl Reduction
Cyp3a22
Hydroxylation
Mequindox
Issue Date2011
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/catcom
Citation
Catalysis Communications, 2011, v. 12 n. 7, p. 637-643 How to Cite?
Abstract
The anti-bacterial agent mequindox is widely used as an animal feed additive in China. Its potential effect on host cells, however, remains largely unknown. Here, we report that pig CYP3A22 represents an important metabolic enzyme in mequindox catalysis. Interestingly, we found that ectopic expression of CYP3A22 reversed the mequindox-induced G2 cell cycle accumulation in cultured pig hepatocytes. To further probe the catalytic mechanism of CYP3A22 in mequindox metabolism, we identified 2′-acetyl-hydroxylation as a major catalytic step of CYP3A22-dependent mequindox metabolism using LC-MS/MS spectrometry. Together, our study suggests that CYP3A22 plays an important role in mequindox metabolism via 2′-acetyl-hydroxylation. © 2010 Elsevier B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/149755
ISSN
2013 Impact Factor: 3.320
2013 SCImago Journal Rankings: 1.270
ISI Accession Number ID
Funding AgencyGrant Number
National Basic Research Program of China (973 Program)2009CB118802
Guangdong Province Universities and Colleges Pearl River Scholar Funded Scheme
Program for New Century Excellent Talents in UniversityNCET-08-0643
Guangdong Province Universities and Colleges Special Funds for Talents Introduction
Funding Information:

This work was supported by the National Basic Research Program of China (973 Program), No: 2009CB118802; the Guangdong Province Universities and Colleges Pearl River Scholar Funded Scheme (2009); the Program for New Century Excellent Talents in University, No: NCET-08-0643; and the Guangdong Province Universities and Colleges Special Funds for Talents Introduction (2008).

References

 

Author Affiliations
  1. The University of Hong Kong
  2. South China Agricultural University
DC FieldValueLanguage
dc.contributor.authorLiu, Jen_US
dc.contributor.authorGe, Xen_US
dc.contributor.authorOuyang, Men_US
dc.contributor.authorTang, Xen_US
dc.contributor.authorWu, Jen_US
dc.contributor.authorWang, Jen_US
dc.contributor.authorJiang, Jen_US
dc.contributor.authorHuen, MSYen_US
dc.contributor.authorDeng, Yen_US
dc.date.accessioned2012-06-26T05:58:08Z-
dc.date.available2012-06-26T05:58:08Z-
dc.date.issued2011en_US
dc.identifier.citationCatalysis Communications, 2011, v. 12 n. 7, p. 637-643en_US
dc.identifier.issn1566-7367en_US
dc.identifier.urihttp://hdl.handle.net/10722/149755-
dc.description.abstractThe anti-bacterial agent mequindox is widely used as an animal feed additive in China. Its potential effect on host cells, however, remains largely unknown. Here, we report that pig CYP3A22 represents an important metabolic enzyme in mequindox catalysis. Interestingly, we found that ectopic expression of CYP3A22 reversed the mequindox-induced G2 cell cycle accumulation in cultured pig hepatocytes. To further probe the catalytic mechanism of CYP3A22 in mequindox metabolism, we identified 2′-acetyl-hydroxylation as a major catalytic step of CYP3A22-dependent mequindox metabolism using LC-MS/MS spectrometry. Together, our study suggests that CYP3A22 plays an important role in mequindox metabolism via 2′-acetyl-hydroxylation. © 2010 Elsevier B.V. All rights reserved.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/catcomen_US
dc.relation.ispartofCatalysis Communicationsen_US
dc.subjectCarbonyl Reductionen_US
dc.subjectCyp3a22en_US
dc.subjectHydroxylationen_US
dc.subjectMequindoxen_US
dc.titleCatalytic characteristics of CYP3A22-dependent mequindox detoxificationen_US
dc.typeArticleen_US
dc.identifier.emailHuen, MSY:huen.michael@hku.hken_US
dc.identifier.authorityHuen, MSY=rp01336en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.catcom.2010.12.029en_US
dc.identifier.scopuseid_2-s2.0-78651097502en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-78651097502&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume12en_US
dc.identifier.issue7en_US
dc.identifier.spage637en_US
dc.identifier.epage643en_US
dc.identifier.isiWOS:000287839600016-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridLiu, J=36739597900en_US
dc.identifier.scopusauthoridGe, X=36739013900en_US
dc.identifier.scopusauthoridOuyang, M=36606787500en_US
dc.identifier.scopusauthoridTang, X=36606961700en_US
dc.identifier.scopusauthoridWu, J=36740582300en_US
dc.identifier.scopusauthoridWang, J=36740542200en_US
dc.identifier.scopusauthoridJiang, J=24776301400en_US
dc.identifier.scopusauthoridHuen, MSY=23004751500en_US
dc.identifier.scopusauthoridDeng, Y=7401531432en_US
dc.identifier.citeulike8624091-

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