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A Study Of Inactive Enzyme-Homologues: The Biochemical And Biological Function Of Ecm14 In Saccharomyces Cerevisiae, Robert Christian Mcdonald
A Study Of Inactive Enzyme-Homologues: The Biochemical And Biological Function Of Ecm14 In Saccharomyces Cerevisiae, Robert Christian Mcdonald
Master's Theses
Like most major enzyme families, the M14 family of metallocarboxypeptidases (MCPs) contains several pseudoenzymes predicted to lack enzyme activity and with unknown molecular function. The genome of the yeast Saccharomyces cerevisiae encodes only one member of the M14 MCP family, a pseudoenzyme named Ecm14 proposed to function in the extracellular matrix. Ecm14 is found throughout ascomycete fungi, with a group of related pseudoenzymes found in basidiomycetes. Although the prodomain of Ecm14 can be cleaved in vivo and in vitro by endopeptidases, suggesting an activation mechanism, no activity has been detected using standard carboxypeptidase substrates.
In order to examine the function …