Chemical Modification and Amino Acid Sequence of Active Site in Sugar Beet<i>α</i>-Glucosidase

• Iwanami Shunsuke

• Matsui Hirokazu

• Kimura Atsuo

• Ito Hiroyuki

• Mori Haruhide

• Honma Mamoru

• Chiba Seiya

書誌事項

タイトル別名

• Chemical Modification and Amino Acid Sequence of Active Site in Sugar Beet .ALPHA.-Glucosidase.

抄録

The modification of amino acid residues in sugar beet α-glucosidase with conduritol B epoxide (CBE), an affinity labeling reagent, inactivated the enzyme. The inactivation followed pseudo-first-order kinetics. The enzyme was protected from inactivation by a competitive inhibitor, Tris, and the partially inactivated enzymes showed only the decrease of V values and no change in Km value. An ³H-CBE labeled peptide isolated from the digest of the inactivated enzyme with Lys-C protease was sequenced. The -COO - group of Asp was found to be specifically labeled, implicating that it is a catalytic group of the enzyme. The sequence around the essential Asp was determined to be -DGIWIDMNE-, which showed a high homology with those of other α-glucosidases.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 59 (3), 459-463, 1995

  公益社団法人 日本農芸化学会

キーワード

• Organic Chemistry
• Molecular Biology
• Applied Microbiology and Biotechnology
• General Medicine
• Biochemistry
• Analytical Chemistry
• Biotechnology

詳細情報

• CRID: 1390001206474430336
• NII論文ID: 110002677472
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.59.459
• COI: 1:CAS:528:DyaK2MXkvVertLY%3D
• ISSN: 13476947
• ISSN: 09168451
• PubMed: 7766184
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.59.459
• 本文言語コード: en
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