PMID:16546401
| Citation |
Zhao, C, Kumada, Y, Imanaka, H, Imamura, K and Nakanishi, K (2006) Cloning, overexpression, purification, and characterization of O-acetylserine sulfhydrylase-B from Escherichia coli. Protein Expr. Purif. 47:607-13 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1016/j.pep.2006.01.002 |
| Keywords |
Cystathionine beta-Synthase/biosynthesis; Cystathionine beta-Synthase/chemistry; Cystathionine beta-Synthase/genetics; Cystathionine beta-Synthase/isolation & purification; Cysteine Synthase/biosynthesis; Cysteine Synthase/chemistry; Cysteine Synthase/isolation & purification; Electrophoresis, Polyacrylamide Gel; Escherichia coli/chemistry; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/biosynthesis; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/isolation & purification; Plasmids/genetics; Substrate Specificity/physiology |
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