title: Engineered metalloregulation in enzymes.
abstract: Protein engineering of metal-dependent enzyme activity is now possible due to the wealth of information available about metalloproteins. The results emerging from these studies provide insight into our understanding of the chemistry of metals in macromolecular environments as well as the biology of metal-protein interactions.
authors.affiliation: Department of Pharmaceutical Chemistry, University of California, San Francisco 94143.
authors.forename: J N
authors.initials: JN
authors.lastname: Higaki
authors.forename: R J
authors.initials: RJ
authors.lastname: Fletterick
authors.forename: C S
authors.initials: CS
authors.lastname: Craik
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003300:Copper / Q000737:chemistry; D006639:Histidine / Q000737:chemistry; D008667:Metalloproteins / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry* / Q000235:genetics; D015202:Protein Engineering; D016415:Sequence Alignment; D013329:Structure-Activity Relationship; D014357:Trypsin / Q000737:chemistry* / Q000235:genetics; D015032:Zinc / Q000737:chemistry
chemical_list: D008667:Metalloproteins; D006639:Histidine; D003300:Copper; D007703:Peptidyl-Dipeptidase A; D014357:Trypsin; D015032:Zinc