title: Thermostability and reactivity in organic solvent of O-phospho-L-serine sulfhydrylase from hyperthermophilic archaeon Aeropyrum pernix K1.
abstract: O-phospho-l-serine sulfhydrylase (OPSS) from archaeon Aeropyrum pernix K1 is able to synthesize l-cysteine even at 80 °C. In this article, we compared thermal stability and reactivity in organic solvent of OPSS with those of O-acetyl-l-serine sulfhydrylase B (OASS-B) from Escherichia coli. As a result, the thermostability of OPSS was much higher than that of OASS-B. Moreover, the activity of OPSS increased in the reaction mixture containing the organic solvent, such as N, N'-dimethyl formamide and 1,4-dioxane, whereas that of OASS-B gradually decreased as the content of organic solvent increased. From the crystal structural analysis, the intramolecular electrostatic interactions of N-terminal domain in OPSS seemed to be correlated with the tolerance of OPSS to high temperature and organic solvent. These results indicate that OPSS is more superior to OASS-B for the industrial production of l-cysteine and unnatural amino acids that are useful pharmaceuticals in the presence of organic solvent.
authors.affiliation: a Faculty of Bioscience, Laboratory of Molecular Biochemistry , Nagahama Institute of Bio-Science and Technology , Nagahama , Japan.
authors.forename: Takashi
authors.initials: T
authors.lastname: Nakamura
authors.forename: Shinji
authors.initials: S
authors.lastname: Asai
authors.forename: Kaori
authors.initials: K
authors.lastname: Nakata
authors.forename: Kohei
authors.initials: K
authors.lastname: Kunimoto
authors.forename: Masateru
authors.initials: M
authors.lastname: Oguri
authors.forename: Kazuhiko
authors.initials: K
authors.lastname: Ishikawa
mesh_terms: D041522:Aeropyrum / Q000201:enzymology*; D019757:Carbon-Oxygen Lyases / Q000737:chemistry* / Q000378:metabolism; D003545:Cysteine / Q000096:biosynthesis*; D004795:Enzyme Stability; D005285:Fermentation; D007700:Kinetics; D012997:Solvents / Q000737:chemistry; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D012997:Solvents; C503351:O-phosphoserine sulfhydrylase, Aeropyrum pernix; D019757:Carbon-Oxygen Lyases; D003545:Cysteine
keywords: Aeropyrum pernix K1; O-phospho-l-serine sulfhydrylase; electrostatic interaction; hyperthermophilic aerobic archaeon; stability to thermal stress and organic solvent