Importance of Trp139 in the product specificity of a maltooligosaccharide-forming amylase from Bacillus stearothermophilus STB04

The maltooligosaccharide-forming amylase from Bacillus stearothermophilus STB04 (Bst-MFA) randomly cleaves the α-1,4 glycosidic linkages of starch to produce predominantly maltopentaose and maltohexaose. The three-dimensional co-crystal structure of Bst-MFA with acarbose highlighted the stacking int...

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Veröffentlicht in:	Applied microbiology and biotechnology 2019-12, Vol.103 (23-24), p.9433-9442
Hauptverfasser:	Xie, Xiaofang, Qiu, Gaoyuan, Zhang, Ziqian, Ban, Xiaofeng, Gu, Zhengbiao, Li, Caiming, Hong, Yan, Cheng, Li, Li, Zhaofeng
Format:	Artikel
Sprache:	eng
Schlagworte:	Acarbose Alanine Amino Acids - chemistry Amylases Amylases - chemistry Amylases - genetics Bacillus stearothermophilus Binding Sites Biomedical and Life Sciences Biotechnologically Relevant Enzymes and Proteins Biotechnology Crystal structure Enzymes Food science Geobacillus stearothermophilus - enzymology Geobacillus stearothermophilus - genetics Hydrolysis Leucine Life Sciences Microbial Genetics and Genomics Microbiology Models, Molecular Mutagenesis Mutagenesis, Site-Directed Mutation Oligosaccharides Oligosaccharides - biosynthesis Plasmids Proteins Site-directed mutagenesis Stacking Starch Substrate Specificity Substrates Tyrosine
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