Mutational analysis of the integral membrane methyltransferase isoprenylcysteine carboxyl methyltransferase (ICMT) reveals potential substrate binding sites Journal Article

   

Authors:	Diver, M. M.; Long, S. B.
Article Title:	Mutational analysis of the integral membrane methyltransferase isoprenylcysteine carboxyl methyltransferase (ICMT) reveals potential substrate binding sites
Abstract:	Background: Isoprenylcysteine carboxyl methyltransferase (ICMT) is an integral membrane enzyme that modifies CAAX proteins. Results: Mutational analysis has identified residues important for activity and substrate recognition. Conclusion: Crucial residues are found in cytosolic and membrane-embedded regions, consistent with the ability of ICMT to bind both water-soluble and lipophilic substrates. Significance: Insights into the enzymatic mechanism of ICMT may assist with inhibitor development.
Keywords:	mutational analysis; methyltransferases; integral membrane; potential substrate
Journal Title:	Journal of Biological Chemistry
Volume:	289
Issue:	38
ISSN:	0021-9258
Publisher:	American Society for Biochemistry and Molecular Biology
Date Published:	2014-09-19
Start Page:	26007
End Page:	26020
Language:	English
DOI:	10.1074/jbc.M114.585125
PROVIDER:	scopus
PUBMED:	25059662
PMCID:	PMC4176209
DOI/URL:	http://www.scopus.com/inward/record.url?eid=2-s2.0-84907218653&partnerID=40&md5=c5005046c3885fd73d6e2d2469c73d74
Notes:	Export Date: 1 October 2014 -- Source: Scopus

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