Research articles
ScienceAsia 51 (2023): 1-6 |doi:
10.2306/scienceasia1513-1874.2023.088
Characterization of a novel bifunctional glutathione
synthetase derived from Enterococcus italicus
Jing Lia,*,?, Lei Yanga,?, Hao Wangb,?, Xueyang Lia, Conghui Zhanga, Kai Tiana, Xue Yanga, Jianyu Zhenga,
Yuese Liua, Meina Zhanga, Guisheng Jiaa, Xiaofeng Zhanga
ABSTRACT: Glutathione is a tripeptide containing a ?-amide bond and a sulfhydryl group, which is composed of
glutamic acid, cysteine, and glycine. It possesses various important biological functions such as antioxidation. Its
biosynthesis initially occurs through the action of glutamate cysteine ligase, which catalyzes the linkage of glutamic
acid and cysteine to form ?-glutamylcysteine, and then glutathione synthetase catalyzes the addition of glycine to
?-glutamylcysteine to form ?-glutamylcysteine glycine. In this study, a strain with high glutathione production was
isolated andidentifiedasEnterococcusitalicus through16SrRNAgenesequencing. The1600bpbifunctionalglutathione
synthetase encoding gene gshF wasobtainedbyPCRandheterogeneouslyexpressedinEscherichiacoli BL21(DE3)using
a pET-22b(+) vector. After purification by Ni column, the molecular weight of bifunctional glutathione synthetase GshF
wasdeterminedtobe60kDa. EnzymaticanalysisshowedthattheoptimumreactiontemperatureofGshFwas37?Cand
the optimum pH was 8.0. Moreover, 30 mmol/l Mg2+ significantly enhanced enzyme activity. These results provided a
basis for understanding the mechanism of high glutathione production in E. italicus and offered a new enzyme source
for glutathione biosynthesis.
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| a |
Technical Center for Safety of Industrial Products, Tianjin Customs, Tianjin 300308 China |
| b |
Department of Critical Care Medicine, Central Hospital of Cangzhou City, Hebei 061000 China |
* Corresponding author, E-mail: lj12345678901201@163.com
Received 23 Dec 2024, Accepted 0 0000
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