Cloning and characterization of antioxidant enzyme methionine sulfoxide-S-reductase from Caenorhabditis elegans

Byung Cheon Lee; Yong Kwon Lee; Ho Joung Lee; Earl R. Stadtman; Kweon Haeng Lee; Namhyun Chung

doi:10.1016/j.abb.2004.11.012

Cloning and characterization of antioxidant enzyme methionine sulfoxide-S-reductase from Caenorhabditis elegans

Byung Cheon Lee, Yong Kwon Lee, Ho Joung Lee, Earl R. Stadtman, Kweon Haeng Lee, Namhyun Chung

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

15 Citations (Scopus)

Abstract

Methionine (Met) residues in proteins are susceptible to oxidation. The resulting methionine sulfoxide can be reduced back to methionine by methionine sulfoxide-S-reductase (MsrA). The MsrA gene, isolated from Caenorhabditis elegans, was cloned and expressed in Escherichia coli. The resultant enzyme was able to revert both free Met and Met in proteins in the presence of either NADPH or dithiothreitol (DTT). However, approximately seven times higher enzyme activity was observed in the presence of DTT than of NADPH. The enzyme had an absolute specificity for the reduction of l-methionine-S-sulfoxide but no specificity for the R isomer. K _m and k _cat values for the enzyme were ∼1.18 mM and 3.64 min ^-1, respectively. Other kinetics properties of the enzyme were also evaluated.

Original language	English
Pages (from-to)	275-281
Number of pages	7
Journal	Archives of Biochemistry and Biophysics
Volume	434
Issue number	2
DOIs	https://doi.org/10.1016/j.abb.2004.11.012
Publication status	Published - 2005 Feb 15

Bibliographical note

Funding Information:
The research was supported in part by an intramural research fund from Korea University, Seoul, Korea.

Copyright:
Copyright 2011 Elsevier B.V., All rights reserved.

Keywords

Caenorhabditis elegans
Catalytic efficiency
Methionine sulfoxide
Methionine-S-sulfoxide reductase
MsrA

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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10.1016/j.abb.2004.11.012

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title = "Cloning and characterization of antioxidant enzyme methionine sulfoxide-S-reductase from Caenorhabditis elegans",

abstract = "Methionine (Met) residues in proteins are susceptible to oxidation. The resulting methionine sulfoxide can be reduced back to methionine by methionine sulfoxide-S-reductase (MsrA). The MsrA gene, isolated from Caenorhabditis elegans, was cloned and expressed in Escherichia coli. The resultant enzyme was able to revert both free Met and Met in proteins in the presence of either NADPH or dithiothreitol (DTT). However, approximately seven times higher enzyme activity was observed in the presence of DTT than of NADPH. The enzyme had an absolute specificity for the reduction of l-methionine-S-sulfoxide but no specificity for the R isomer. K m and k cat values for the enzyme were ∼1.18 mM and 3.64 min -1, respectively. Other kinetics properties of the enzyme were also evaluated.",

keywords = "Caenorhabditis elegans, Catalytic efficiency, Methionine sulfoxide, Methionine-S-sulfoxide reductase, MsrA",

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AU - Lee, Byung Cheon

AU - Lee, Yong Kwon

AU - Lee, Ho Joung

AU - Stadtman, Earl R.

AU - Lee, Kweon Haeng

AU - Chung, Namhyun

PY - 2005/2/15

Y1 - 2005/2/15

N2 - Methionine (Met) residues in proteins are susceptible to oxidation. The resulting methionine sulfoxide can be reduced back to methionine by methionine sulfoxide-S-reductase (MsrA). The MsrA gene, isolated from Caenorhabditis elegans, was cloned and expressed in Escherichia coli. The resultant enzyme was able to revert both free Met and Met in proteins in the presence of either NADPH or dithiothreitol (DTT). However, approximately seven times higher enzyme activity was observed in the presence of DTT than of NADPH. The enzyme had an absolute specificity for the reduction of l-methionine-S-sulfoxide but no specificity for the R isomer. K m and k cat values for the enzyme were ∼1.18 mM and 3.64 min -1, respectively. Other kinetics properties of the enzyme were also evaluated.

AB - Methionine (Met) residues in proteins are susceptible to oxidation. The resulting methionine sulfoxide can be reduced back to methionine by methionine sulfoxide-S-reductase (MsrA). The MsrA gene, isolated from Caenorhabditis elegans, was cloned and expressed in Escherichia coli. The resultant enzyme was able to revert both free Met and Met in proteins in the presence of either NADPH or dithiothreitol (DTT). However, approximately seven times higher enzyme activity was observed in the presence of DTT than of NADPH. The enzyme had an absolute specificity for the reduction of l-methionine-S-sulfoxide but no specificity for the R isomer. K m and k cat values for the enzyme were ∼1.18 mM and 3.64 min -1, respectively. Other kinetics properties of the enzyme were also evaluated.

KW - Caenorhabditis elegans

KW - Catalytic efficiency

KW - Methionine sulfoxide

KW - Methionine-S-sulfoxide reductase

KW - MsrA

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JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

IS - 2

ER -

Cloning and characterization of antioxidant enzyme methionine sulfoxide-S-reductase from Caenorhabditis elegans

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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