Substrate specificity of an esterase from the archaeon Sulfolobus tokodaii bearing a GGG(A)X motif

Reina Wada; Masanaru Ozaki; Takashi Kumon; Hiromichi Ohta; Kenji Miyamoto

doi:10.3109/10242422.2015.1095679

Substrate specificity of an esterase from the archaeon Sulfolobus tokodaii bearing a GGG(A)X motif

Reina Wada, Masanaru Ozaki, Takashi Kumon, Hiromichi Ohta, Kenji Miyamoto

Department of Biosciences and Informatics

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

Abstract

A GGG(A)X-type esterase (Est0071) from an archaeon catalyzes asymmetric hydrolysis of prochiral bulky malonic diesters in good enantioselectivity. The selectivity of Est0071 was for the opposite enantiomer to that previously shown for pig liver esterase, and the resulting enantiomeric excess of the products was higher. Est0071 could also catalyze the hydrolysis of various acetates of secondary alcohols, and showed moderate enantioselectivity in these reactions.

Original language	English
Pages (from-to)	188-190
Number of pages	3
Journal	Biocatalysis and Biotransformation
Volume	33
Issue number	3
DOIs	https://doi.org/10.3109/10242422.2015.1095679
Publication status	Published - 2015 May 4

Keywords

Esterase
GGG(A)X-motif
Sulfolobus tokodaii
hydrolysis
malonic diester

ASJC Scopus subject areas

Biotechnology
Catalysis
Biochemistry

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10.3109/10242422.2015.1095679

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title = "Substrate specificity of an esterase from the archaeon Sulfolobus tokodaii bearing a GGG(A)X motif",

abstract = "A GGG(A)X-type esterase (Est0071) from an archaeon catalyzes asymmetric hydrolysis of prochiral bulky malonic diesters in good enantioselectivity. The selectivity of Est0071 was for the opposite enantiomer to that previously shown for pig liver esterase, and the resulting enantiomeric excess of the products was higher. Est0071 could also catalyze the hydrolysis of various acetates of secondary alcohols, and showed moderate enantioselectivity in these reactions.",

keywords = "Esterase, GGG(A)X-motif, Sulfolobus tokodaii, hydrolysis, malonic diester",

author = "Reina Wada and Masanaru Ozaki and Takashi Kumon and Hiromichi Ohta and Kenji Miyamoto",

note = "Publisher Copyright: {\textcopyright} 2015 Taylor & Francis.",

year = "2015",

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doi = "10.3109/10242422.2015.1095679",

language = "English",

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T1 - Substrate specificity of an esterase from the archaeon Sulfolobus tokodaii bearing a GGG(A)X motif

AU - Wada, Reina

AU - Ozaki, Masanaru

AU - Kumon, Takashi

AU - Ohta, Hiromichi

AU - Miyamoto, Kenji

PY - 2015/5/4

Y1 - 2015/5/4

N2 - A GGG(A)X-type esterase (Est0071) from an archaeon catalyzes asymmetric hydrolysis of prochiral bulky malonic diesters in good enantioselectivity. The selectivity of Est0071 was for the opposite enantiomer to that previously shown for pig liver esterase, and the resulting enantiomeric excess of the products was higher. Est0071 could also catalyze the hydrolysis of various acetates of secondary alcohols, and showed moderate enantioselectivity in these reactions.

AB - A GGG(A)X-type esterase (Est0071) from an archaeon catalyzes asymmetric hydrolysis of prochiral bulky malonic diesters in good enantioselectivity. The selectivity of Est0071 was for the opposite enantiomer to that previously shown for pig liver esterase, and the resulting enantiomeric excess of the products was higher. Est0071 could also catalyze the hydrolysis of various acetates of secondary alcohols, and showed moderate enantioselectivity in these reactions.

KW - Esterase

KW - GGG(A)X-motif

KW - Sulfolobus tokodaii

KW - hydrolysis

KW - malonic diester

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DO - 10.3109/10242422.2015.1095679

M3 - Article

AN - SCOPUS:84945901797

SN - 1024-2422

VL - 33

SP - 188

EP - 190

JO - Biocatalysis and Biotransformation

JF - Biocatalysis and Biotransformation

IS - 3

ER -

Substrate specificity of an esterase from the archaeon Sulfolobus tokodaii bearing a GGG(A)X motif

Abstract

Keywords

ASJC Scopus subject areas

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