Substrate Specificity Study of Recombinant Rhizopus Chinensis Aspartic Proteinase
Rhizopuspepsin, a model aspartic proteinase from the fungus Rhizopus chinensis, has recently been cloned and expressed by Chen et al. (1991). High resolution crystallographic analysis of rhizopuspepsin and complexes with active site ligands has been reported by Davies’ group (Parris et al., this volume). Our initial characterization of the substrate specificity of the active site is described in this report. This study will enable future comparisons between kinetic and crystallographic data from other aspartic proteinases as well as for use in planning and analyzing site-directed mutagenesis studies.
KeywordsAspartic Proteinase 8452A Diode Array 8452A Diode Array Spectrophotometer Oklahoma Medical Research Foundation Carboxyl Proteinase
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