Glutaredoxin-like protein (GLP)—a novel bacteria sulfurtransferase that protects cells against cyanide and oxidative stresses

Paula, Carla Peres de; Santos, M. C. dos; Tairum, Carlos A.; Breyer, Carlos Alexandre; Toledo-Silva, Guilherme; Toyama, Marcos H.; Mori, Gustavo Maruyama; Oliveira, Marcos Aurélio Farias de

doi:10.1007/s00253-020-10491-5

Cited by 3 publications

(1 citation statement)

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“…Many studies suggest, in fact, that the proteins have roles in ‘managing’ stress tolerance and in maintaining redox homeostasis [ 63 , 72 , 73 ]. TST is also able to degrade reactive oxygen species (ROS) with thioredoxin in cell-free systems [ 74 , 75 ]. Analyses of TST expression and activity also revealed that it was overexpressed in MST-knockout mice in order to compensate for the effect of the MST deficiency [ 76 ].…”

Section: Structure and Function Of Tstmentioning

confidence: 99%

Thiosulfate-Cyanide Sulfurtransferase a Mitochondrial Essential Enzyme: From Cell Metabolism to the Biotechnological Applications

Buonvino

Arciero

Melino

2022

IJMS

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Thiosulfate: cyanide sulfurtransferase (TST), also named rhodanese, is an enzyme widely distributed in both prokaryotes and eukaryotes, where it plays a relevant role in mitochondrial function. TST enzyme is involved in several biochemical processes such as: cyanide detoxification, the transport of sulfur and selenium in biologically available forms, the restoration of iron–sulfur clusters, redox system maintenance and the mitochondrial import of 5S rRNA. Recently, the relevance of TST in metabolic diseases, such as diabetes, has been highlighted, opening the way for research on important aspects of sulfur metabolism in diabetes. This review underlines the structural and functional characteristics of TST, describing the physiological role and biomedical and biotechnological applications of this essential enzyme.

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