Acid carboxypeptidase from a wood-deteriorating basidiomycete, Pycnoporus Sanguineus |
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Authors: | Eiji Ichishima Kenichiro Yoshimura Katsumi Tomoda |
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Institution: | 1. Laboratory of Enzymology and Microbial Chemistry, Tokyo Nōkō University, Fuchu, Tokyo 183, Japan;1. Research Laboratories of Fermentation Products, Takeda Chemical Injustries Ltd., Osaka 532, Japan |
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Abstract: | An acid carboxypeptidase (EC 3.4.16.1) has been isolated from the culture filtrate of a wood-degrading Basidiomycete, Pycnoporus sanguineus and the molecular and enzymatic properties of the enzyme were determined. The extracellular acid carboxypeptidase was homogeneous on polyacrylamide gel electrophoresis at pH 9.4 and SDS-disc gel electrophoresis. The MWs as determined by gel filtration and SDS-gel electrophoresis were 50 000 and 54 000, respectively. The isoelectric point was pH 4.78 using electrofocusing. The purified enzyme had a pH optimum of 3.4, a Km of 0.74 mM and a kcat of 16/sec with benzyloxycarbonyl-l-glutamyl-l-tyrosine. The Km and kcat values for bradykinin at pH 3.4 and 30° were 2.0 mM and 25/sec. Values for angiotensin at pH 3.4 and 30° were 0.76 mM and 2.4/sec, respectively. |
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Keywords: | Basidiomycete wood-rotting fungi acid carboxypeptidase carboxypeptidase |
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