Replacement of Loops at the Entrance of the Active Pocket of <i>Streptococcus thermophilus</i> 4,6-α-Glucanotransferase Changes Its Catalytic Activity and Product Specificity-Reference-Cited by-同舟云学术

Replacement of Loops at the Entrance of the Active Pocket of Streptococcus thermophilus 4,6-α-Glucanotransferase Changes Its Catalytic Activity and Product Specificity

Published:2024-05-24 Issue:22 Volume:72 Page:12607-12617
ISSN:0021-8561
Container-title:Journal of Agricultural and Food Chemistry
language:en
Short-container-title:J. Agric. Food Chem.

Author:

Li Dan¹²^ORCID,Xu Wenqi¹,Mu Siyu¹,Gao Xusheng¹,Ma Fumin¹,Duan Cuicui¹,Li Xiaolei¹²^ORCID

Affiliation:

1. Key Laboratory of Agro-products Processing Technology, Education Department of Jilin Province, Changchun University, 6543 Weixing Road, Changchun 130022, People’s Republic of China

2. Key Laboratory of Intelligent Rehabilitation and Barrier-free For the Disabled, Ministry of Education, Changchun University, 6543 Weixing Road, Changchun 130022, People’s Republic of China

Funder

Department of Science and Technology of Jilin Province

Changchun University

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jafc.4c00803

Reference36 articles.

1. Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of -amylase-related proteins

2. 4,6-α-Glucanotransferase, a Novel Enzyme That Structurally and Functionally Provides an Evolutionary Link between Glycoside Hydrolase Enzyme Families 13 and 70

3. Structure of the α-1,6/α-1,4-specific glucansucrase GTFA fromLactobacillus reuteri121

4. Remarkable evolutionary relatedness among the enzymes and proteins from the α-amylase family

5. Crystal structure of a 117 kDa glucansucrase fragment provides insight into evolution and product specificity of GH70 enzymes