Identification of Ionizable Groups Essential to the Activity of Isomalto-dextranase from Arthrobacter globiformis
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概要
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The active site of isomalto-dextranase from Arthrobacter globiformis was investigated by kinetic and chemical-modification methods. The ionization constants, pK_e1 and pK_e2, of the essential ionizable groups 1 and 2 of the free enzyme were 3.3 and 6.3 for dextran T2000 and 3.5 and 6.1 for isomaltotriose. The PK_e1 and PK_e2 both shifted to higher PH when the dielectric constant of the reaction mixture decreased. The heats of ionization for groups 1 and 2 were 0 kcal/mol or less with both substrates. These kinetic results suggested that the ionizable groups essential for the enzyme activity were carboxyl and carboxylate. Modification with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, modifying carboxyl residues specifically, resulted in inactivation of the enzyme, and isomaltotriose protected the enzyme against such inactivation. These findings also indicated that the carboxyl groups were essential to the enzyme activity.
- 社団法人日本農芸化学会の論文
- 1994-11-23
著者
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木村 淳夫
北海道大学大学院農学研究院応用生命科学部門
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Chiba Seiya
Department Of Agricultural Chemistry Faculty Of Agriculture Hokkaido University
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Chiba Seiya
Division Of Applied Bioscience Graduate School Of Agriculture Hokkaido University
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KIMURA Atsuo
Department of Applied Bioscience, Graduate School of Agriculture, Hokkaido University
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TAKAYANAGI Tsutomu
Department of Agricultural Chemistry, Faculty of Agriculture, Hokkaido University
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Okada Gentaro
Department of Biology, Faculty of Education, Shizuoka University
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Kimura Atsuo
Department Of Agricultural Chemistry Faculty Of Agriculture Hokkaido University
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岡田 嚴太郎
Shizuoka Univ. Shizuoka Jpn
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Kimura Atsuo
Hokkaido University
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Takayanagi T
Interdisciplinary Graduate School Of Medicine And Engineering & The Institute Of Enology And Vit
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Okada Gentaro
Department Of Biology Faculty Of Education Shizuoka University
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