Presence of a dipeptidyl aminopeptidase III in Saccharomyces cerevisiae.
The soluble fraction of a cell extract of Saccharomyces cerevisiae was found to contain hydrolytic activity toward arginyl-arginyl-beta-naphthylamide (Arg-Arg-beta NA). Most of the contaminating Arg-beta NA hydrolysis activity was removed by diethylaminoethyl (DEAE)-cellulose column chromatography and the enzyme was partially purified. It is very similar in various properties to mammalian dipeptidyl aminopeptidase III (DAP III), although it differs slightly in some respects.
Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Japan.
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Watanabe
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Kumagai
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Fujimoto
D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C100152:dipeptidyl peptidase III