Publications

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Journal Article
Palmer, M. A. et al. Biosynthetic thiolase from Zoogloea ramigera. Evidence for a mechanism involving Cys-378 as the active site base. J Biol Chem 266, 8369-75 (1991).
Davis, J. T. et al. Biosynthetic thiolase from zoogloea ramigera. I. Preliminary characterization and analysis of proton transfer reaction. J Biol Chem 262, 82-9 (1987).
Davis, J. T. et al. Biosynthetic thiolase from Zoogloea ramigera. II. Inactivation with haloacetyl CoA analogs. J Biol Chem 262, 90-6 (1987).
Peoples, O. P., Masamune, S., Walsh, C. T. & Sinskey, A. J. Biosynthetic thiolase from Zoogloea ramigera. III. Isolation and characterization of the structural gene. J Biol Chem 262, 97-102 (1987).
Williams, S. F. et al. Biosynthetic thiolase from Zoogloea ramigera. Mutagenesis of the putative active-site base Cys-378 to Ser-378 changes the partitioning of the acetyl S-enzyme intermediate. J Biol Chem 267, 16041-3 (1992).
Thompson, S. et al. Mechanistic studies on beta-ketoacyl thiolase from Zoogloea ramigera: identification of the active-site nucleophile as Cys89, its mutation to Ser89, and kinetic and thermodynamic characterization of wild-type and mutant enzymes. Biochemistry 28, 5735-42 (1989).
Gerngross, T. U. et al. Overexpression and purification of the soluble polyhydroxyalkanoate synthase from Alcaligenes eutrophus: evidence for a required posttranslational modification for catalytic activity. Biochemistry 33, 9311-20 (1994).