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  • Title: Cloning, overexpression, purification, and characterization of O-acetylserine sulfhydrylase-B from Escherichia coli.
    Author: Zhao C, Kumada Y, Imanaka H, Imamura K, Nakanishi K.
    Journal: Protein Expr Purif; 2006 Jun; 47(2):607-13. PubMed ID: 16546401.
    Abstract:
    O-Acetylserine sulfhydrylase-B (OASS-B, EC 2.5.1.47) is one of the two isozymes produced by Escherichia coli that catalyze the synthesis of L-cysteine from O-acetyl-L-serine and sulfide. The cysM gene encoding OASS-B was cloned and the enzyme was overexpressed in E. coli using pUC19 with a lacUV5 promoter. The enzyme was purified to homogeneity, as evidenced by SDS-PAGE. Approximately 300 mg of purified OASS-B was obtained from 1600 mL of culture broth with a purification yield of 60% or higher. The purified OASS-B was characterized and its properties compared with OASS-A. OASS-B did not form a complex with E. coli serine acetyltransferase (SAT, EC 2.3.1.30) and showed a wide range of substrate specificity in nonproteinaceous amino acid synthesis.
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