The cystathionase-rhodanese system

Szczepkowski, T; Wood, John L.

doi:10.1016/0005-2744(67)90050-2

Cited by 70 publications

(36 citation statements)

References 18 publications

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“…These results seem to be logically consistent because CSE catalyzes, inter alia, reactions yielding sulfane sulfur–containing products (thiocysteine, thiocystine) [25,26]. Moreover, Iciek et al indicated that DADS and DATS elevated the total sulfane sulfur level and the activity of sulfane sulfur biosynthetic enzymes in the mouse liver cells [27].…”

Section: Discussionmentioning

confidence: 80%

The Effects of Different Garlic-Derived Allyl Sulfides on Anaerobic Sulfur Metabolism in the Mouse Kidney

Iciek¹,

Bilska‐Wilkosz²,

Górny³

et al. 2016

Antioxidants

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Diallyl sulfide (DAS), diallyl disulfide (DADS) and diallyl trisulfide (DATS) are major oil-soluble organosulfur compounds of garlic responsible for most of its pharmacological effects. The present study investigated the influence of repeated intraperitoneally (ip) administration of DAS, DADS and DATS on the total level of sulfane sulfur, bound sulfur (S-sulfhydration) and hydrogen sulfide (H2S) and on the activity of enzymes, which catalyze sulfane sulfur formation and transfer from a donor to an acceptor in the normal mouse kidney, i.e., γ-cystathionase (CSE) and rhodanese (TST). The activity of aldehyde dehydrogenase (ALDH), which is a redox-sensitive protein, containing an –SH group in its catalytic center, was also determined. The obtained results indicated that all tested compounds significantly increased the activity of TST. Moreover, DADS and DATS increased the total sulfane sulfur level and CSE activity in the normal mouse kidney. ALDH activity was inhibited in the kidney after DATS administration. The results indicated also that none of the studied allyl sulfides affected the level of bound sulfur or H2S. Thus, it can be concluded that garlic-derived DADS and DATS can be a source of sulfane sulfur for renal cells but they are not connected with persulfide formation.

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Section: Discussionmentioning

confidence: 80%

The Effects of Different Garlic-Derived Allyl Sulfides on Anaerobic Sulfur Metabolism in the Mouse Kidney

Iciek¹,

Bilska‐Wilkosz²,

Górny³

et al. 2016

Antioxidants

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“…Rhodanese [54], cystathionine γ -lyase [78], and thioredoxin reductase (EC 2.8.1.5) [79] also form persulfide intermediates in their catalytic processes. These enzymes cooperate in cyanide detoxification [75,[80][81][82][83][84]. Mercaptopyruvate sulfurtransferase, cystathionine γ -lyase, and thioredoxin reductase act in the cytosol, and mercaptopyruvate sulfurtransferase, rhodanese, and thioredoxin reductase act in the mitochondria.…”

Section: Cyanide Detoxification By Mercaptopy-ruvate Sulfurtransferasementioning

confidence: 99%

The Mercaptopyruvate Pathway in Cysteine Catabolism: A Physiologic Role and Related Disease of the Multifunctional 3-Mercaptopyruvate Sulfurtransferase

Nagahara

Sawada²

2006

CMC

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The conversion of cysteine to 3-sulfino-alanine is a major pathway in cysteine catabolism. Cysteine dioxygenase catalyzes the reaction and dietary intake of the essential amino acid methionine and the semi-essential amino acid cysteine increases the level of this enzyme by suppressing enzyme degradation via polyubiquitination. The production of cellular antioxidants such as glutathione, thioredoxin, and their families is important in cysteine metabolism, and these cellular antioxidants have critical roles in the maintenance of the cellular redox status. The mercaptopyruvate pathway, in which cysteine or aspartate transaminase catalyzes the transamination from cysteine to 3-mercaptopyruvate and then 3-mercaptopyruvate sulfurtransferase catalyzes the transsulfuration from 3-mercaptopyruvate to pyruvate, also contributes to maintain the cellular redox. 3-Mercaptopyruvate sulfurtransferase serves as an antioxidant protein: when the enzyme is exposed to stoichiometric amounts of the oxidant hydrogen peroxide, it is inhibited via the formation of low redox sulfenate at the catalytic site cysteine. On the other hand, activity is restored by the reductant dithiothreitol or reduced thioredoxin. 3-Mercaptopyruvate sulfurtransferase also detoxifies cyanide via transsulfuration from a stable persulfide at the catalytic site cysteine, a reaction intermediate, suggesting that cyanide detoxification is not necessarily an enzymatic reaction. Furthermore, a congenital defect of the enzyme causes mercaptolactate-cysteine disulfiduria associated with or without mental retardation, although the pathogenesis remains unclear. These facts suggest that 3-mercaptopyruvate sulfurtransferase has physiologic roles as an antioxidant and a cyanide antidote; is essential for neural function, and participates in cysteine degradation.

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“…Production of pyruvate and reduced inorganic sulphur from cysteine can occur by two known pathways of cysteine metabolism in mammalian tissues. These are the cleavage of cyst(e)ine by cystathionase [EC 4.4.1.1;cyst(e)ine desulphhydrase] (Cavallini et al, 1962a,b;Szczepkowski & Wood, 1967;Yamanishi & Tuboi, 1981) and the transamination of cysteine to 3-mercaptopyruvate followed by transsulphuration or desulphuration of 3-mercaptopyruvate (Ubuka et al, 1977a(Ubuka et al, ,b, 1978.…”

Section: Introductionmentioning

confidence: 99%

Metabolism of cysteine in rat hepatocytes. Evidence for cysteinesulphinate-independent pathways

Drake

Rosa

Stipanuk

1987

Biochemical Journal

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The metabolism of cysteine and cysteinesulphinate was studied in freshly isolated rat hepatocytes. Over 80O% of the 14CO2 formed from [1-14C]cysteinesulphinate could be accounted for by production of hypotaurine plus taurine in incubations of rat hepatocytes with either 1 mm-or 25 mM-cysteinesulphinate. In similar incubations with 1 mm-or 25 mM-cysteine, less than 10% of 14CO2 evolution from [1-14C]cysteine could be accounted for by production of hypotaurine plus taurine. In incubations with cysteine, but not with cysteinesulphinate, the production of urea and ammonia was substantially increased above that observed in incubations without substrate. Addition of unlabelled cysteinesulphinate did not affect 14C02 production from [1-14C]cysteine. Addition of 2-oxoglutarate resulted in a marked increase in cysteinesulphinate catabolism via the transamination pathway, but addition of neither 2-oxoglutarate nor pyruvate to the incubation system had any effect on cysteine catabolism. Inhibition of cystathionase with propargylglycine decreased 14CO2 production from [1-14C]cysteine about 50% and markedly decreased production ofammonia plus urea N; cysteinesulphinate catabolism was not affected. These data suggest that a substantial proportion of cysteine is catabolized by cysteinesulphinate-independent pathways in the rat hepatocyte and, furthermore, that cleavage of cyst(e)ine by cystathionase may be an important physiological pathway for cysteine catabolism in rat liver.

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The cystathionase-rhodanese system

Cited by 70 publications

References 18 publications

The Effects of Different Garlic-Derived Allyl Sulfides on Anaerobic Sulfur Metabolism in the Mouse Kidney

The Effects of Different Garlic-Derived Allyl Sulfides on Anaerobic Sulfur Metabolism in the Mouse Kidney

The Mercaptopyruvate Pathway in Cysteine Catabolism: A Physiologic Role and Related Disease of the Multifunctional 3-Mercaptopyruvate Sulfurtransferase

Metabolism of cysteine in rat hepatocytes. Evidence for cysteinesulphinate-independent pathways

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