Structural elements in dextran glucosidase responsible for high specificity to long chain substrate

Biochimica Et Biophysica Acta
Wataru SaburiAtsuo Kimura

Abstract

Dextran glucosidase from Streptococcus mutans (SMDG) and Bacillus oligo-1,6-glucosidases, members of glycoside hydrolase family 13 enzymes, have the high sequence similarity. Each of them is specific to alpha-1,6-glucosidic linkage at the non-reducing end of substrate to liberate glucose. The activities toward long isomaltooligosaccharides were different in both enzymes, in which SMDG and oligo-1,6-glucosidase showed high and low activities, respectively. We determined the structural elements essential for high activity toward long-chain substrate. From conformational comparison between SMDG and B. cereus oligo-1,6-glucosidase (three-dimensional structure has been solved), Trp238 and short beta-->alpha loop 4 of SMDG were considered to contribute to the high activity to long-chain substrate. W238A had similar kcat/Km value for isomaltotriose to that for isomaltose, suggesting that the affinity of subsite +2 was decreased by Trp238 replacement. Trp238 mutants as well as the chimeric enzyme having longer beta-->alpha loop 4 of B. subtilis oligo-1,6-glucosidase showed lower preference for long-chain substrates, indicating that both Trp238 and short beta-->alpha loop 4 were important for high activity to long-chain substrates.

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Citations

Sep 5, 2007·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Wataru SaburiAtsuo Kimura
Nov 11, 2008·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Keizo YamamotoShigeyoshi Osaki
Jun 10, 2015·Acta Crystallographica. Section D, Biological Crystallography·Xing ShenMin Yao
May 4, 2016·Cellular and Molecular Life Sciences : CMLS·Masayuki OkuyamaAtsuo Kimura
May 4, 2016·Cellular and Molecular Life Sciences : CMLS·Marie Sofie MøllerBirte Svensson
Aug 9, 2011·Bioscience, Biotechnology, and Biochemistry·Momoko KobayashiAtsuo Kimura
Mar 31, 2019·Biotechnology Letters·So-Jin YangYoung-Min Kim
Jun 16, 2016·The Journal of Biological Chemistry·Takayoshi TagamiAtsuo Kimura
May 29, 2018·Bioscience, Biotechnology, and Biochemistry·Patcharapa KlahanAtsuo Kimura

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