Kinetic studies on the glutathione peroxidase activity of selenium-containing glutathione transferase

Huijun Yu; Junqiu Liu; Xiaoman Liu; Tianzhu Zang; Guimin Luo; Jiacong Shen

doi:10.1016/j.cbpc.2005.05.003

Kinetic studies on the glutathione peroxidase activity of selenium-containing glutathione transferase

Huijun Yu
, Junqiu Liu^*
, Xiaoman Liu
, Tianzhu Zang
, Guimin Luo
, Jiacong Shen

^*Corresponding author for this work

Jilin University

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

14 Scopus citations

Abstract

Selenium-containing glutathione transferase (seleno-GST) was generated by biologically incorporating selenocysteine into the active site of glutathione transferase (GST) from a blowfly Lucilia cuprina (Diptera: Calliphoridae). Seleno-GST mimicked the antioxidant enzyme glutathione peroxidase (GPx) and catalyzed the reduction of structurally different hydroperoxides by glutathione. Kinetic investigations reveal a ping-pong kinetic mechanism in analogy with that of the natural GPx cycle as opposed to the sequential one of the wild type GST. This difference of the mechanisms might result from the intrinsic chemical properties of the incorporated residue selenocysteine, and the selenium-dependent mechanism is suggested to contribute to enhancement of the enzymatic efficiency.

Original language	English
Pages (from-to)	382-389
Number of pages	8
Journal	Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology
Volume	141
Issue number	3
DOIs	https://doi.org/10.1016/j.cbpc.2005.05.003
State	Published - Jul 2005
Externally published	Yes

Keywords

Enzyme mimics
Glutathione peroxidase
Kinetics
Mechanism
Selenium
Selenium-containing glutathione transferase
Selenium-containing glutathione transferase from Lucilia cuprina
Selenocysteine

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10.1016/j.cbpc.2005.05.003

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title = "Kinetic studies on the glutathione peroxidase activity of selenium-containing glutathione transferase",

abstract = "Selenium-containing glutathione transferase (seleno-GST) was generated by biologically incorporating selenocysteine into the active site of glutathione transferase (GST) from a blowfly Lucilia cuprina (Diptera: Calliphoridae). Seleno-GST mimicked the antioxidant enzyme glutathione peroxidase (GPx) and catalyzed the reduction of structurally different hydroperoxides by glutathione. Kinetic investigations reveal a ping-pong kinetic mechanism in analogy with that of the natural GPx cycle as opposed to the sequential one of the wild type GST. This difference of the mechanisms might result from the intrinsic chemical properties of the incorporated residue selenocysteine, and the selenium-dependent mechanism is suggested to contribute to enhancement of the enzymatic efficiency.",

keywords = "Enzyme mimics, Glutathione peroxidase, Kinetics, Mechanism, Selenium, Selenium-containing glutathione transferase, Selenium-containing glutathione transferase from Lucilia cuprina, Selenocysteine",

author = "Huijun Yu and Junqiu Liu and Xiaoman Liu and Tianzhu Zang and Guimin Luo and Jiacong Shen",

year = "2005",

month = jul,

doi = "10.1016/j.cbpc.2005.05.003",

language = "英语",

volume = "141",

pages = "382--389",

journal = "Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology",

issn = "1096-4959",

publisher = "Elsevier Inc.",

number = "3",

}

TY - JOUR

T1 - Kinetic studies on the glutathione peroxidase activity of selenium-containing glutathione transferase

AU - Yu, Huijun

AU - Liu, Junqiu

AU - Liu, Xiaoman

AU - Zang, Tianzhu

AU - Luo, Guimin

AU - Shen, Jiacong

PY - 2005/7

Y1 - 2005/7

N2 - Selenium-containing glutathione transferase (seleno-GST) was generated by biologically incorporating selenocysteine into the active site of glutathione transferase (GST) from a blowfly Lucilia cuprina (Diptera: Calliphoridae). Seleno-GST mimicked the antioxidant enzyme glutathione peroxidase (GPx) and catalyzed the reduction of structurally different hydroperoxides by glutathione. Kinetic investigations reveal a ping-pong kinetic mechanism in analogy with that of the natural GPx cycle as opposed to the sequential one of the wild type GST. This difference of the mechanisms might result from the intrinsic chemical properties of the incorporated residue selenocysteine, and the selenium-dependent mechanism is suggested to contribute to enhancement of the enzymatic efficiency.

AB - Selenium-containing glutathione transferase (seleno-GST) was generated by biologically incorporating selenocysteine into the active site of glutathione transferase (GST) from a blowfly Lucilia cuprina (Diptera: Calliphoridae). Seleno-GST mimicked the antioxidant enzyme glutathione peroxidase (GPx) and catalyzed the reduction of structurally different hydroperoxides by glutathione. Kinetic investigations reveal a ping-pong kinetic mechanism in analogy with that of the natural GPx cycle as opposed to the sequential one of the wild type GST. This difference of the mechanisms might result from the intrinsic chemical properties of the incorporated residue selenocysteine, and the selenium-dependent mechanism is suggested to contribute to enhancement of the enzymatic efficiency.

KW - Enzyme mimics

KW - Glutathione peroxidase

KW - Kinetics

KW - Mechanism

KW - Selenium

KW - Selenium-containing glutathione transferase

KW - Selenium-containing glutathione transferase from Lucilia cuprina

KW - Selenocysteine

UR - https://www.scopus.com/pages/publications/20544458738

U2 - 10.1016/j.cbpc.2005.05.003

DO - 10.1016/j.cbpc.2005.05.003

M3 - 文章

C2 - 15949961

AN - SCOPUS:20544458738

SN - 1096-4959

VL - 141

SP - 382

EP - 389

JO - Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology

JF - Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology

IS - 3

ER -

Kinetic studies on the glutathione peroxidase activity of selenium-containing glutathione transferase

Abstract

Keywords

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