title: Design of allosterically regulated protein catalysts.
abstract: Activity of allosteric protein catalysts is regulated by an external stimulus, such as protein or small molecule binding, light activation, pH change, etc., at a location away from the active site of the enzyme. Since its original introduction in 1961, the concept of allosteric regulation has undergone substantial expansion, and many, if not most, enzymes have been shown to possess some degree of allosteric regulation. The ability to create new catalysts that can be turned on and off using allosteric interactions would greatly expand the chemical biology toolbox and will allow for detection of environmental pollutants and disease biomarkers and facilitate studies of cellular processes and metal homeostasis. Thus, design of allosterically regulated protein catalysts represents an actively growing area of research. In this paper, we describe various approaches to achieving regulation of catalysis.
authors: Department of Chemistry, Syracuse University , 111 College Place, Syracuse, New York 13244, United States.
authors: Olga V
authors: OV
authors: Makhlynets
authors: Elizabeth A
authors: EA
authors: Raymond
authors: Ivan V
authors: IV
authors: Korendovych
mesh_terms: D000494:Allosteric Regulation; D000495:Allosteric Site; D000818:Animals; D055162:Biocatalysis; D020134:Catalytic Domain; D006801:Humans; D008958:Models, Molecular; D015202:Protein Engineering / Q000379:methods; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D011993:Recombinant Fusion Proteins