Distribution of Cysteine Desulfhydrase in Microorganisms

Ohkishi, Haruyuki; Nishikawa, Daikichiro; Kumagai, Hidehiko; Yamada, Hideaki

doi:10.1080/00021369.1981.10864500

Cited by 8 publications

(9 citation statements)

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“…Analyses of the isotopic distributions of 2H and/or 34S in the bound serine, cysteine, and methionine were performed by GC-MS of the N-trifluoroacetyl n-butyl ester derivative of methionine, the N,O-trifluoroacetyl n-butyl ester derivative of serine, and the S-methyl-N-trifluoroacetyl n-butyl ester derivative of cysteine. (Brueggeman et al, 1962;Wiebers & Garner, 1967); (d) cysteine desulfhydrase (Fromageot, 1951;Ohkishi et al, 1981); (e) enzymatic or nonenzymatic reductive cleavage by intracellular thiols, Le., glutathione (Flavin, 1962); (f) 0-cystathionase (Flavin & Slaughter, 1964;Delavier-Klutchko & Flavin, 1965b); (g) decomposition into sulfane sulfur and cysteine (Flavin, 1962); (h) transamination (Rudman & Meister, 1953); (i) mercaptopyruvate sulfurtransferase (Meister et al, 1954;Vachek & Wood, 1972); 6) reduction of sulfane sulfur [So] to sulfide catalyzed by sulfane reductase. The reaction could proceed with or without the involvement of rhodanese (Westley, 1981).…”

Section: Methodsmentioning

confidence: 97%

Metabolism of L-[sulfane-34S]thiocystine by Escherichia coli

White¹

1982

Biochemistry

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The metabolism of L-thiocystine [bis(2-amino-2-carboxyethyl) trisulfide] by Escherichia coli was studied by using L-[sulfane-35S]thiocystine. This compound was found to serve as a source of sulfur for E. coli grown on a defined medium free of other sulfur sources and to incorporate its labeled sulfur into cysteine as well as the other sulfur-containing cellular components. For determination of the extent of the synthesis of new cysteine in these cells, cells were grown with [3,3-2H2]serine and L-[sulfane-34S]thiocystine, and the extent of incorporation of both deuterium and 34S into the cellular cysteine was measured by gas chromatography-mass spectrometry. The results show that approximately 50% of the cysteine which is incorporated into cellular macromolecules is derived from the thiocystine without cleavage of the carbon-sulfur bond, the remaining portion being newly biosynthesized from serine and 34S-enriched H2S. These results suggest that the first step in the metabolism of thiocystine by E. coli involves the beta elimination of pyruvate. This type of reaction is characteristic of the cleavage reactions catalyzed by beta-cystathionase.

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Section: Methodsmentioning

confidence: 97%

Metabolism of L-[sulfane-34S]thiocystine by Escherichia coli

White¹

1982

Biochemistry

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“…It is likely that the microorganisms selected for in this work did not represent the spectrum of microorganisms in the same relative proportions as existed in the soil samples. The enzyme cysthathionine -y-lyase appears to be more prevalent in the actinomycetes and fungi (30), whereas cysteine desulfhydrase appears to be mainly of bacterial origin (26,31). We may have selected a large bacterial component in our enrichment cultures and thus that microbial group primarily responsible for cysteine desulfhydrase production.…”

Section: Downloaded Frommentioning

confidence: 99%

“…Thiocysteine then reacts nonenzymatically with cysteine or other sulfhydryl-containing compounds to yield H2S and cystine. Cysteine desulfhydrase activity was found to be widespread in bacteria and present in 1 of 27 fungal strains, but not present in 14 strains of actinomycetes and 30 strains of yeasts (26,31). In contrast, cystathionine -y-lyase activity has been found mainly in actinomycetes and eucaryotic microorganisms (11,30).…”

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confidence: 99%

Mechanisms of H ₂ S Production from Cysteine and Cystine by Microorganisms Isolated from Soil by Selective Enrichment

Morra

Dick

1991

Appl Environ Microbiol

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Hydrogen sulfide (H2S) is a major component of biogenic gaseous sulfur emissions from terrestrial environments. However, little is known concerning the pathways for H2S production from the likely substrates, cysteine and cystine. A mixed microbial culture obtained from cystine-enriched soils was used in assays (50 min, 37°C) with 0.05 M Tris-HCl (pH 8.5), 25 i,mol of L-cysteine, 25 ,imol of L-cystine, and 0.04 ,mol of pyridoxal 5'-phosphate. Sulfide was trapped in a center well containing zinc acetate, while pyruvate was measured by derivatization with 2,4-dinitrophenylhydrazine. Sulfide and total pyruvate production were 17.6 and 17.2 nmol mg of proteinmmi', respectively. Dithiothreitol did not alter reaction stoichiometry or the amount of H2S and total pyruvate, whereas N-ethylmaleimide reduced both H2S and total pyruvate production equally. The amount of H2S produced was reduced by 96% when only L-cystine was included as the substrate in the assay and by 15% with the addition of propargylglycine, a specific suicide inhibitor of cystathionine

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“…Controls lacking substrate, or containing substrate but not sand were included, and all assays were incubated at 37~ Arylsulphohydrolase activity was assayed using p-nitrophenyl sulphate (1 ml, 5 mM) as substrate and acetate buffer (4ml, 0.5 M, pH 5.8) 13 and thiosulphate sulphurtransferase by the method of Tabatabai and Singh 14. Cysteine desulphohydrase was assayed following a modification of the method of Ohkishi et al 8. Reaction mixtures contained sand (1 g); tris-HCl buffer (3 ml, 0.2 M, pH 8.3); L-cysteine (1 ml, 5 mM in Tris-HC1 buffer) and pyridoxal-phosphate (1 ml, 0.2 M in Tris-HCl buffer).…”

Section: Enzyme Assaysmentioning

confidence: 99%

Assay and properties of some sulphur enzymes in coastal sands

Skiba

Wainwright

1983

Plant Soil

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SummaryArylsulphohydrolase; cysteine desulphohydrase and thiosulphate cyanide sulphurtransferase were assayed in coastal sands and their properties determined. Low enzyme activity was detected in sands lacking vegetation, but much higher activities were detected in the rhizospheres of climax vegetation; Hippopha~ rhamnoides and Ammophila sp. Properties of the enzymes were generally similar to those quoted for the enzymes in soils.

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Distribution of Cysteine Desulfhydrase in Microorganisms

Cited by 8 publications

References 0 publications

Metabolism of L-[sulfane-34S]thiocystine by Escherichia coli

Metabolism of L-[sulfane-34S]thiocystine by Escherichia coli

Mechanisms of H ₂ S Production from Cysteine and Cystine by Microorganisms Isolated from Soil by Selective Enrichment

Assay and properties of some sulphur enzymes in coastal sands

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Distribution of Cysteine Desulfhydrase in Microorganisms

Cited by 8 publications

References 0 publications

Metabolism of L-[sulfane-34S]thiocystine by Escherichia coli

Metabolism of L-[sulfane-34S]thiocystine by Escherichia coli

Mechanisms of H 2 S Production from Cysteine and Cystine by Microorganisms Isolated from Soil by Selective Enrichment

Assay and properties of some sulphur enzymes in coastal sands

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Mechanisms of H ₂ S Production from Cysteine and Cystine by Microorganisms Isolated from Soil by Selective Enrichment