Impact on Substrate Specificity of Mutational Subsite Isozyme Mimicry in Barley α-Amylase

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概要

• 論文の詳細を見る

• The mutational analysis of the roles of specific side chains at individual subsites have been conducted for barley α-amylase 1(AMY1) across the ten subsites long substrate binding cleft. The present study specifically focuses on such mutants in which the AMY2 structure has been mimicked. Generally the kinetics parameters for mutants at subsites accommodating the substrate glycone part showed decreased affinity for oligosaccharide and amylose DP 17 whereas an aglycon binding subsite +4 AMY2 mimic had increased affinity but reduced activity. Among barley α-amylase/subtilisin inhibitor (BASI) recognition mimics, further more mutation at one site provided weak inhibition of an otherwise insensitive AMYL type hybrid, whereas a mimic in another area of the protein-protein interface was not affected by BASI.

• 日本応用糖質科学会の論文
• 2003-07-14

著者

• Bak‐jensen K

  Carlsberg Lab. Copenhagen Valby Dnk

• Bak-jensen Kristian

  Department Of Chemistry Carlsberg Laboratory

• Svensson B

  Department Of Chemistry Carlsberg Laboratory

• MORI Haruhide

  Department of Applied Bioscience, Graduate School of Agriculture, Hokkaido University

• JENSEN Morten

  Department of Chemistry, Carlsberg Laboratory

• Jensen Morten

  Department Of Chemistry Carlsberg Laboratory

• Svensson Birte

  Department Of Chemistr Carlsberg Laboratory

• Mori H

  Department Of Chemistry Carlsberg Laboratory

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