Structure-activity studies on the retinal rod outer segment isoprenylated protein methyltransferase
In: Journal of the American Chemical Society, Jg. 114 (1992), Heft 10, S. 3966-3973
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Zugriff:
Structure-activity studies were performed on the retinal rod outer segment isoprenylated protein methyltransferase that transfers a methyl group from S-adenosylmethionine (AdoMet) to the carboxyl group of isoprenylated (farnesylated or geranylgeranylated) cysteine residues. This methyltransferase enzyme has been shown to methylate N-acetyl-S-farnesyl-L-cysteine (L-AFC, 1) and S-(farnesyl-3-thio)propionic acid (FTP, 2). It is shown here that the enzyme does not enzymatically process D-AFC (8), although D-AFC (8) is a mixed-type inhibitor of the enzyme.
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Structure-activity studies on the retinal rod outer segment isoprenylated protein methyltransferase
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Autor/in / Beteiligte Person: | GILBERT, B. A ; ENG WUI, TAN ; PEREZ-SALA, D ; RANDO, R. R |
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Zeitschrift: | Journal of the American Chemical Society, Jg. 114 (1992), Heft 10, S. 3966-3973 |
Veröffentlichung: | Washington, DC: American Chemical Society, 1992 |
Medientyp: | academicJournal |
Umfang: | print, 50 ref |
ISSN: | 0002-7863 (print) |
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