Literature DB >> 25779754

Thermostability and reactivity in organic solvent of O-phospho-L-serine sulfhydrylase from hyperthermophilic archaeon Aeropyrum pernix K1.

Takashi Nakamura1, Shinji Asai, Kaori Nakata, Kohei Kunimoto, Masateru Oguri, Kazuhiko Ishikawa.   

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.

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Keywords:  Aeropyrum pernix K1; O-phospho-l-serine sulfhydrylase; electrostatic interaction; hyperthermophilic aerobic archaeon; stability to thermal stress and organic solvent

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Year:  2015        PMID: 25779754     DOI: 10.1080/09168451.2015.1020753

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  1 in total

1.  Role of F225 in O-phosphoserine sulfhydrylase from Aeropyrum pernix K1.

Authors:  Emi Takeda; Kohei Kunimoto; Yoshito Kawai; Misumi Kataoka; Kazuhiko Ishikawa; Takashi Nakamura
Journal:  Extremophiles       Date:  2016-07-05       Impact factor: 2.395

  1 in total

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