Substrate inactivation of bacterial l-aspartate α-decarboxylase from Corynebacterium jeikeium K411 and improvement of molecular stability by saturation mutagenesis-Reference-Cited by-同舟云学术

Substrate inactivation of bacterial l-aspartate α-decarboxylase from Corynebacterium jeikeium K411 and improvement of molecular stability by saturation mutagenesis

Published:2019-03-28 Issue:4 Volume:35 Page:
ISSN:0959-3993
Container-title:World Journal of Microbiology and Biotechnology
language:en
Short-container-title:World J Microbiol Biotechnol

Author:

Mo Qin,Mao An,Li Youran,Shi Guiyang

Funder

the National Science and Technology Major Project

the National Natural Foundation of China

national first-class discipline program of Light Industry Technology and Engineering

Science and Technology Support Program of Jiangsu Province

Publisher

Springer Science and Business Media LLC

Subject

Applied Microbiology and Biotechnology,General Medicine,Physiology,Biotechnology

Link

http://link.springer.com/content/pdf/10.1007/s11274-019-2629-6.pdf

Reference24 articles.

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3. Chen X, Li Y, Gu Z, Ding Z, Zhang L, Shi G (2017) Expression and characterization of two l-aspartate alpha-decarboxylases. Microbiol China 44:2337–2344. https://doi.org/10.13344/j.microbiol.china.170009

4. Cronan JE (1980) Beta-alanine synthesis in Escherichia coli. J Bacteriol 141:1291–1297

5. Cui W, Shi Z, Fang Y, Zhou L, Ding N, Zhou Z (2014) Significance of Arg3, Arg54, and Tyr58 of l-aspartate alpha-decarboxylase from Corynebacterium glutamicum in the process of self-cleavage. Biotechnol Lett 36:121–126. https://doi.org/10.1007/s10529-013-1337-9

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