Structure-Functional Examination of Cysteine Synthase A (CysK) from <i>Limosilactobacillus reuteri</i> LR1.

ABSTRACT: This study presents a comprehensive analysis of cysteine synthase A (CysK) from Limosilactobacillus reuteri LR1 (LreCysK), an enzyme involved in the biosynthesis of L-cysteine. This protein supports crucial cellular functions such as sulfur metabolism, antioxidant defense, detoxification, and protein synthesis. Previously, the gene encoding LreCysK was cloned, and the enzyme with His-tag on the N-terminus was obtained in active and soluble form. Here, kinetic parameters of the enzyme were determined by the previously developed high-pressure liquid chromatography (HPLC) and ninhydrin methods. It was found that LreCysK has similar K_M^OAS and k_cat as CysKs from Escherichia coli and from the model plant Arabidopsis thaliana. The therm

SUBMITTER: Pometun AA 

PROVIDER: S-EPMC12785664 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature