N-terminal domain truncation yielded a unique dimer of polysaccharide hydrolase with enhanced enzymatic activity, stability and calcium ion independence-Reference-Cited by-同舟云学术

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N-terminal domain truncation yielded a unique dimer of polysaccharide hydrolase with enhanced enzymatic activity, stability and calcium ion independence

Published:2024-05 Issue: Volume:266 Page:131352
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Xiang La,Hu Xinlin,Du Chao,Wu Lian,Lu Zhenghui,Zhou Jiahai,Zhang Guimin

Funder

National Natural Science Foundation of China

Fundamental Research Funds for the Central Universities

Ministry of Education of the People's Republic of China

Ministry of Science and Technology of the People's Republic of China

National Key Research and Development Program of China

Publisher

Elsevier BV

Reference36 articles.

1. Global distribution of carbohydrate utilization potential in the prokaryotic tree of life;López-Mondéjar;mSystems,2022

2. Halophiles 2010: life in saline environments;Ma;Appl. Environ. Microbiol.,2010

3. Structural basis for the aminoacid composition of proteins from halophilic archea;Tadeo;PLoS Biol.,2009

4. Molecular adaptation: the malate dehydrogenase from the extreme halophilic bacterium Salinibacter ruber behaves like a non-halophilic protein;Madern;Biochimie,2004

5. Functional characterization and crystal structure of thermostable amylase from Thermotoga petrophila, reveals high thermostability and an unusual form of dimerization;Hameed;BBA Proteins Proteom.,1865

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