title: Thiol modification of diacylglycerol kinase: dependence upon site membrane disposition and reagent hydrophobicity.
abstract: Reaction rates were determined between disulfide reagents of varying hydrophobicity and single-cysteine mutants of diacylglycerol kinase, an integral membrane protein. Polar reagents reacted most rapidly with surface-exposed sites. However, a very non-polar reagent also reacted more rapidly with exposed cysteines than with membrane sites. Moreover, this non-polar reagent usually reacted more slowly with membrane sites than did more polar reagents. These results are consistent with the notion that disulfide exchange reactions involving buried cysteines of diacylglycerol kinase are very slow in the membrane interior, such that the competing rates of reactions which occur when normally buried cysteine sites make motional excursions to hydrated regions of the interface can be significant.
authors.affiliation: Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH 44107-4970, USA.
authors.forename: L
authors.initials: L
authors.lastname: Czerski
authors.forename: C R
authors.initials: CR
authors.lastname: Sanders
mesh_terms: D000595:Amino Acid Sequence; D003545:Cysteine / Q000737:chemistry; D019852:Diacylglycerol Kinase / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry*; D004228:Dithionitrobenzoic Acid / Q000737:chemistry; D008969:Molecular Sequence Data; D013438:Sulfhydryl Compounds / Q000737:chemistry*
chemical_list: D004220:Disulfides; D013438:Sulfhydryl Compounds; D004228:Dithionitrobenzoic Acid; D019852:Diacylglycerol Kinase; D003545:Cysteine