Molecular mechanism for the substrate specificity of Arthrobacter globiformis M6 α-glucosidase CmmB, belonging to glycoside hydrolase family 13 subfamily 30-Reference-Cited by-同舟云学术

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Molecular mechanism for the substrate specificity of Arthrobacter globiformis M6 α-glucosidase CmmB, belonging to glycoside hydrolase family 13 subfamily 30

Published:2024-10 Issue: Volume:61 Page:104516
ISSN:2212-4292
Container-title:Food Bioscience
language:en
Short-container-title:Food Bioscience

Author:

Saburi Wataru^ORCID,Tagami Takayoshi,Usui Takuya,Yu Jian,Ose Toyoyuki,Yao Min^ORCID,Mori Haruhide^ORCID

Funder

Japan Agency for Medical Research and Development

Publisher

Elsevier BV

Reference59 articles.

1. Phenix: A comprehensive Python-based system for macromolecular structure solution;Adams;Acta Crystallographica Section D Biolgical Crystallography,2010

2. Function and structure of GH13_31 α-glucosidase with high α-(1→4)-glucosidic linkage specificity and transglucosylation activity;Auiewiriyanukul;FEBS Letters,2018

3. Subsite mapping of the human pancreatic α-amylase active site through structural, kinetic, and mutagenesis techniques;Brayer;Biochemistry,2000

4. BoGH13ASus from Bacteroides ovatus represents a novel α-amylase used for Bacteroides starch breakdown in the human gut;Brown;Cellular and Molecular Life Sciences,2023

5. Structure of the Aspergillus oryzae α-amylase complexed with the inhibitor acarbose at 2.0 Å resolution;Brzozowski;Biochemistry,1997

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