DECARBOXYLASE

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Identification of key residues for the activity of aspartate 4‑decarboxylase towards l‑3‑methylaspartate
《Systems Microbiology and Biomanufacturing》2023年第3期449-456,共8页Mingzhu Hao Laichuang Han Zhemin Zhou Zhongmei Liu 
the National Natural Science Foundation of China(21878125).
Aspartate 4-decarboxylase(ASD)has been modified to obtain the catalytic ability of the unnatural substrate l-3-methylaspartate.However,the mechanism remains to be clarified.In the present study,the semi-rational modif...
关键词：Aspartate 4-decarboxylase l-3-methylasparte Substrate-binging pocket Molecular dynamics simulation 
Isolation and mechanism analysis of a catalytic efciency improved L‑aspartateβ‑decarboxylase toward 3‑methylaspartic acid被引量：1
《Systems Microbiology and Biomanufacturing》2022年第1期157-164,共8页Yufeng Liu Mingzhu Hao Zhemin Zhou Zhongmei Liu 
This work was supported by National Key R&D Program of China(2017YFE0129600);the National Natural Science Foundation of China(21878125);the Priority Academic Program Development of Jiangsu Higher Education Institutions,the 111 Project(No.111-2-06).
L-Aspartateβ-decarboxylase from Acinetobacter radioresistens(ArASD)has been modifed to convert 3-methylaspartic acid into 2-aminobutyric acid,which activated a novel process for biosynthesis of 2-aminobutyric acid.Ho...
关键词：L-Aspartateβ-decarboxylase 3-Methylasparic acid The internal aldimine Enzyme engineering Molecular dynamics simulation 
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