Characterization of D-Alanyl-(D)-meso-2, 6-diaminopimelic Acid Endopeptidase from Streptomyces globisporus 1829
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概要
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D-Alanyl-(D)-meso-2, 6-diaminopimelic acid endopeptidase was purified 47.4-fold with a yield of 40.5% from mutanolysin, which was partially purified from the cultural supernatant of Streptomyces globisporus 1829, by using ion exchange column chromatographies and a molecular sieve column. The purified enzyme was electrophoretically homogeneous. This enzyme had a molecular weight of 13, 500 and an isoelectric point ofpI9.0. This enzyme was most active at pH8.5 and stable between pHs 8.0 and 9.0. The hydrolyzing activity of this enzyme was enhanced by Co++ and Ca++ but inhibited appreciably by Zn++, Cu++ and EDTA. The enzyme activity was not affected by β-lactam antibiotics and vancomycin. The Km values for bisdisaccharide heptapeptide and its derivative modified chemically by BOC-S were calculated to be 5.7×10-4 and 4.0×10-4M, respectively.
- 社団法人 日本農芸化学会の論文
著者
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TAKAHASHI Eiji
Research Alliance, University of Tsukuba
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YOKOGAWA Kanae
Research Laboratory, Dainippon Pharmaceutical Co., Ltd.
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Kawata Shigeo
Research Information Center Institute Of Plasma Physics Nagoya University
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KAWATA Shigeo
Research Laboratories, Dainippon Pharmaceutical Co., Ltd.
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TAKASE Yoshiyuki
Research Laboratories, Dainippon Pharmaceutical Co., Ltd.
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YOKOGAWA Kanae
Research Laboratories, Dainippon Pharmaceutical Co.
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