Thiosulphate-Sulphur Transferase (Rhodanese) Deficiency in Leber's Hereditary Optic Atrophy

Cagianut, B.; Rhyner, K; W, Furrer; Schnebli, Hans Peter

doi:10.1016/s0140-6736(81)91171-5

Cited by 34 publications

(3 citation statements)

References 2 publications

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“…The dysfunction of NADH: ubiquinone oxidoreductase due to LHON mutations leads to the overproduction of ROS which, in turn, triggers a series of mitochondrial dysfunctions that eventually result in the death of retinal ganglion cells via apoptosis [ 108 , 109 ]. A pronounced reduction in TST activity was found in liver biopsies [ 110 ] from Leber patients suggesting a role of TST in this disease. Moreover, the deficiency of the cyanide detoxification pathway plays a role in disease progression.…”

Section: Tst In Diseasesmentioning

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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Section: Tst In Diseasesmentioning

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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“…Rhodanese concentration in a liver biopsy from one patient was normal (Wilson, 1965). Unfortunately, techniques of assay of mercapto-pyruvate transulphurase, the proximate enzyme in the conversion of cysteine to thiosulphate, have not been applied to the small quantities of tissue available, but recently, Swiss workers using a more refined extraction procedure have presented good evidence of rhodanese deficiency in liver biopsies from two patients with Leber's disease (Cagianut et al, 1981).…”

Section: Leber's Diseasementioning

confidence: 99%

Brain disorders in relation to biochemical lesions

Wilson

1982

J of Inher Metab Disea

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ConclusionThe paediatric neurologist confronted with an array of named and unnamed heredo‐degenerative disorders, as yet undefined biochemically, is continually frustrated by the therapeutic nihilism and by genetic counselling based on a statistical estimate of risk. Regrettably, clinical observation has provided few clues so far with which to direct research, but since further technical innovation is unlikely to provide helpful answers unless the appropriate questions are asked, it is essential that we go on trying to formulate proper questions.

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“…This function is more prominent in mammals where highly cytotoxic cyanide is converted to a less toxic thiosulphate and excreted through the kidney (Bourdoux et al, 1980;Cagianut et al, 1984;Keith et al, 1989;Fagbounka et al, 2004). In plants, a close relationship exists between rhodanese activity and cyanogenesis, which suggests that the enzyme provides a mechanism for cyanide detoxification in cyanogenic plants (Smith and Urbanska, 1986).…”

Section: Introductionmentioning

confidence: 99%

Physicochemical properties of rhodanese: A cyanide detoxifying enzyme from Pentadiplandra brazzeana (Baill) root

Raphael¹,

Bamidele²,

Leonard³

et al. 2017

Afr. J. Biotechnol.

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Rhodanese a ubiquitous sulphur transferase enzyme catalyses the detoxification of cyanide to a less toxic thiocyanate. Rhodanese from the root of Pentadiplandra brazzeana was purified by ammonium sulphate precipitation and affinity chromatography. The enzyme had a specific activity of 4.82 RU/mg of protein. The K m values of the substrates (KCN and Na 2 S 2 O 3 ) were 11.76 and 10 mM, respectively. The optimum pH and temperature of the enzyme activity were 8.0 and 60°C, respectively. The enzyme was not inhibited by the heavy metals (BaCl 2 , KCl, NiCl 2 , NaCl, MnCl 2 , and ZnCl 2 ). This study affirmed the presence of rhodanese in the root of P. brazzeana, an indication that the plant may be of useful biotechnological application, especially in bioremediation of cyanide intoxified farm sites.

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Thiosulphate-Sulphur Transferase (Rhodanese) Deficiency in Leber's Hereditary Optic Atrophy

Cited by 34 publications

References 2 publications

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

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

Brain disorders in relation to biochemical lesions

Physicochemical properties of rhodanese: A cyanide detoxifying enzyme from Pentadiplandra brazzeana (Baill) root

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