Biosynthesis of α-keto acids and resolution of chiral amino acids by l-amino acid deaminases from Proteus mirabilis.

Autor: Chang J; School of Food and Bioengineering, Hefei University of Technology, Feicui Road, No.420, Hefei, Anhui, China., Zhang Y; School of Food and Bioengineering, Hefei University of Technology, Feicui Road, No.420, Hefei, Anhui, China. Electronic address: 1346637312@qq.com., Li Z; School of Food and Bioengineering, Hefei University of Technology, Feicui Road, No.420, Hefei, Anhui, China. Electronic address: 553326402@qq.com., Ma Y; Anhui Anlito Biotechnology Co., Ltd., Lvan, Anhui, China. Electronic address: hr@horaechina.com., Hu X; School of Food and Bioengineering, Hefei University of Technology, Feicui Road, No.420, Hefei, Anhui, China. Electronic address: huxq@hfut.edu.cn., Yang J; School of Food and Bioengineering, Hefei University of Technology, Feicui Road, No.420, Hefei, Anhui, China; Anhui Anlito Biotechnology Co., Ltd., Lvan, Anhui, China. Electronic address: jwyang@hfut.edu.cn., Zhang H; School of Food and Bioengineering, Hefei University of Technology, Feicui Road, No.420, Hefei, Anhui, China. Electronic address: hbzhang@hfut.edu.cn.
Jazyk: angličtina
Zdroj: Protein expression and purification [Protein Expr Purif] 2024 Sep; Vol. 221, pp. 106518. Date of Electronic Publication: 2024 May 29.
DOI: 10.1016/j.pep.2024.106518
Abstrakt: Chiral amino acids and their deamination products, α-keto acids, have important applications in food, medicine, and fine chemicals. In this study, two l-amino acid deaminase genes from Proteus mirabilis, PM473 of type Ⅰ and PM471 of type Ⅱ were cloned and expressed in Escherichia coli respectively, expected to achieve the chiral separation of amino acids. Extensive substrate preference testing showed that both deaminases had catalytic effects on the d-amino acid component of the D, l-amino acids, and PM473 has a wider catalytic range for amino acids. When D, L-Cys was used as the substrate, all L-Cys components and 75.1 % of D-Cys were converted to mercapto pyruvate, and the remaining D-Cys was a single chiral enantiomer. Molecular docking analysis showed that the interaction between the substrate and the key residues affected the stereoselectivity of enzymes. The compatibility of hydrophobicity between the binding pocket and substrate may be the basic factor that affects the substrate selectivity. This work provides an alternative method for the production of α-keto acids and the resolution of chiral amino acids.
Competing Interests: Declaration of competing interest All authors agree to publish and declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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