Improvement of catalytic efficiency and thermal stability of l-asparaginase from Bacillus subtilis 168 through reducing the flexibility of the highly flexible loop at N-terminus-Reference-Cited by-同舟云学术

Improvement of catalytic efficiency and thermal stability of l-asparaginase from Bacillus subtilis 168 through reducing the flexibility of the highly flexible loop at N-terminus

Published:2019-03 Issue: Volume:78 Page:42-49
ISSN:1359-5113
Container-title:Process Biochemistry
language:en
Short-container-title:Process Biochemistry

Author:

Feng Yue,Liu Song^ORCID,Pang Cuiping,Gao Hui,Wang Miao,Du Guocheng

Funder

National Natural Science Foundation of China

Key Research and Development Program of Jiangsu Province

Publisher

Elsevier BV

Subject

Applied Microbiology and Biotechnology,Biochemistry,Bioengineering

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4. Glutaminase‐free asparaginase from Vibrio succinogenes: an antilymphoma enzyme lacking hepatotoxicity;Distasio;Int. J. Cancer,1982

5. Engineering the substrate specificity of Escherichia coli asparaginase II. Selective reduction of glutaminase activity by amino acid replacements at position 248;Derst;Protein Sci.,2000

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