Improved enantioselectivity of thermostable esterase ST0071 from archaeon Sulfolobus tokodaii by site-saturation mutagenesis

Masanaru Ozaki, Norifumi Kawakami, Hiromichi Ohta, Kenji Miyamoto

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

An archaeon GGG(A)X-type esterase (ST0071) can catalyze the hydrolysis of various acetates of secondary alcohols, but shows low enantioselectivity. Using structure-guided site-saturation mutagenesis, we successfully identified a G274W variant that has excellent selectivity compared with that of wild-type ST0071.

Original languageEnglish
Pages (from-to)249-252
Number of pages4
JournalBiocatalysis and Biotransformation
Volume34
Issue number5
DOIs
Publication statusPublished - 2016 Sep 2

Fingerprint

Sulfolobus
Mutagenesis
Enantioselectivity
Archaea
Esterases
Hydrolysis
Acetates
Alcohols

Keywords

  • directed evolution
  • enantioselectivity
  • esterase
  • Sulfolobus tokodaii

ASJC Scopus subject areas

  • Catalysis
  • Biotechnology
  • Biochemistry

Cite this

Improved enantioselectivity of thermostable esterase ST0071 from archaeon Sulfolobus tokodaii by site-saturation mutagenesis. / Ozaki, Masanaru; Kawakami, Norifumi; Ohta, Hiromichi; Miyamoto, Kenji.

In: Biocatalysis and Biotransformation, Vol. 34, No. 5, 02.09.2016, p. 249-252.

Research output: Contribution to journalArticle

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