Importance of Trp139 in the product specificity of a maltooligosaccharide-forming amylase from Bacillus stearothermophilus STB04-Reference-Cited by-同舟云学术

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

Published:2019-11-01 Issue:23-24 Volume:103 Page:9433-9442
ISSN:0175-7598
Container-title:Applied Microbiology and Biotechnology
language:en
Short-container-title:Appl Microbiol Biotechnol

Author:

Xie Xiaofang,Qiu Gaoyuan,Zhang Ziqian,Ban Xiaofeng,Gu Zhengbiao,Li Caiming,Hong Yan,Cheng Li,Li Zhaofeng

Funder

National Natural Science Foundation of China

China Postdoctoral Science Foundation

Natural Science Foundation of Jiangsu Province

Jiangsu province “Collaborative Innovation Center of Food Safety and Quality Control” industry development program.

Publisher

Springer Science and Business Media LLC

Subject

Applied Microbiology and Biotechnology,General Medicine,Biotechnology

Link

http://link.springer.com/content/pdf/10.1007/s00253-019-10194-6.pdf

Reference47 articles.

1. Aghajari N, Roth M, Haser R (2002) Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic α-amylase. Biochemistry 41(13):4273–4280

2. Agirre J, Moroz O, Meier S, Brask J, Munch A, Hoff T, Andersen C, Wilson KS, Davies GJ (2019) The structure of the AliC GH13 α-amylase from Alicyclobacillus sp. reveals the accommodation of starch branching points in the α-amylase family. Acta Crystallogr D Struct Biol 75(Pt 1):1–7

3. Alikhajeh J, Khajeh K, Ranjbar B, Naderi-Manesh H, Lin YH, Liu E, Guan HH, Hsieh YC, Chuankhayan P, Huang YC, Jeyaraman J, Liu MY, Chen CJ (2010) Structure of Bacillus amyloliquefaciens α-amylase at high resolution: implications for thermal stability. Acta Crystallogr Sect F Struct Biol Cryst Commun 66(Pt 2):121–129

4. Bai Y, Gangoiti J, Dijkstra BW, Dijkhuizen L, Pijning T (2017) Crystal structure of 4,6-α-glucanotransferase supports diet-driven evolution of GH70 enzymes from α-amylases in oral Bacteria. Structure 25(2):231–242

5. Bak-Jensen KS, Andre G, Gottschalk TE, Paes G, Tran V, Svensson B (2004) Tyrosine 105 and threonine 212 at outermost substrate binding subsites -6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of barley α-amylase 1. J Biol Chem 279(11):10093–10102

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3. A novel maltooligosaccharide-forming α-amylase from Bacillus cereus and its application in the preparation of maltopentaose product;Process Biochemistry;2023-05

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