Isolation and mechanism analysis of a catalytic efficiency improved L-aspartate β-decarboxylase toward 3-methylaspartic acid-Reference-Cited by-同舟云学术

登录注册会员服务联系我们

Isolation and mechanism analysis of a catalytic efficiency improved L-aspartate β-decarboxylase toward 3-methylaspartic acid

Published:2021-08-05 Issue:1 Volume:2 Page:157-164
ISSN:2662-7655
Container-title:Systems Microbiology and Biomanufacturing
language:en
Short-container-title:Syst Microbiol and Biomanuf

Author:

Liu Yufeng,Hao Mingzhu,Zhou Zhemin,Liu Zhongmei

Funder

national key r&d program of china

national natural science foundation of china

priority academic program development of jiangsu higher education institutions

the 111 project

Publisher

Springer Science and Business Media LLC

Link

https://link.springer.com/content/pdf/10.1007/s43393-021-00049-5.pdf

Reference20 articles.

1. Wang NC, Lee CY. Molecular cloning of the aspartate 4-decarboxylase gene from Pseudomonas sp. ATCC 19121 and characterization of the bifunctional recombinant enzyme. Appl Microbiol Biotechnol. 2006;73:339–48.

2. Jansonius JN. Structure, evolution and action of vitamin B6-dependent enzymes. Curr Opin Struct Biol. 1998;8:759–69.

3. Dajnowicz S, Parks MJ, Hu X, Gesler K, Andrey Y, Kovalevsky YA, Mueser C. Direct evidence that an extended hydrogen-bonding network influences activation of pyridoxal 5′-phosphate in aspartate aminotransferase. J Biol Chem. 2017;292:5970–80.

4. Chen HJ, Ko TP, Lee CY, Wang NC, Wang AH. Structure, assembly, and mechanism of a PLP-dependent dodecameric L-aspartate beta-decarboxylase. Structure. 2009;17:517–29.

5. Lima S, Sundararaju B, Huang C, Khristoforov R, Momany C, Phillips SR. The crystal structure of the Pseudomonas dacunhae aspartate-b-decarboxylase dodecamer reveals an unknown oligomeric assembly for a pyridoxal-5′-phosphate-dependent enzyme. J Mol Biol. 2009;388:98–108.

Cited by 1 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Identification of key residues for the activity of aspartate 4-decarboxylase towards l-3-methylaspartate;Systems Microbiology and Biomanufacturing;2022-10-17

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线，采集、加工和组织学术论文而形成的新型学术文献查询和分析系统，可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容，当前同舟云学术共收录了国内外主流学术期刊6万余种，收集的期刊论文及会议论文总量共计约1.5亿篇，并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询！咨询电话：010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号京ICP备18003416号-3