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

Bioscience, Biotechnology, and Biochemistry
Takashi NakamuraKazuhiko 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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Citations

Jul 6, 2016·Extremophiles : Life Under Extreme Conditions·Emi TakedaTakashi Nakamura
Feb 11, 2021·Journal of Bioscience and Bioengineering·Emi TakedaTakashi Nakamura

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Methods Mentioned

BETA
PCR
electrophoresis
protein assay

Software Mentioned

Molecular Operating Environment ( MOE
OASS
ProtSA
Protein Contacts panel
OPSS
MOE

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