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  • 1
    Electronic Resource
    Electronic Resource
    l-Cysteine metabolism via 3-mercaptopyruvate pathway and sulfate formation in rat liver mitochondria (1992)
    Springer
    Amino acids 2 (1992), S. 143-155 
    Details
    ISSN: 1438-2199
    Keywords: Amino acids ; Cysteine metabolism ; 3-Mercaptopyruvate pathway ; Sulfate formation ; Mitochondria ; Glutathione
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We have studied the 3-mercaptopyruvate pathway (transamination pathway) ofl-cysteine metabolism in rat liver mitochondria.l-Cysteine and other substrates at 10 mM concentration were incubated with mitochondrial fraction at pH 8.4, and sulfate and thiosulfate were determined by ion chromatography. Whenl-cysteine alone was incubated, sulfate formed was 0.7µmol per mitochondria from one g of liver per 60 min. Addition of 2-oxoglutarate and GSH resulted in more than 3-fold increase in sulfate formation, and thiosulfate was formed besides sulfate. The sum (A + 2B) of sulfate (A) and thiosulfate (B) formed was approximately 7-times that withl-cysteine alone. Incubation with 3-mercaptopyruvate resulted in sulfate and thiosulfate formation, and sulfate was formed with thiosulfate. These reactions were stimulated with glutathione. Sulfate formation froml-cysteinesulfinate and 2-oxoglutarate was not enhanced by glutathione and thiosulfate was not formed. These findings indicate thatl-cysteine was metabolized and sulfate was formed through 3-mercaptopyruvate pathway in mitochondria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00806085
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Inhibition of sulfate-forming activity in rat liver mitochondria by (aminooxy)acetate (1993)
    Springer
    Amino acids 5 (1993), S. 245-251 
    Details
    ISSN: 1438-2199
    Keywords: Amino acids ; Cysteine metabolism ; MP pathway ; Sulfate formation ; (Aminooxy)acetate ; Rat liver mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The effect of (aminooxy)acetate, an inhibitor of aminotransferases, on the sulfate formation froml-cysteine andl-cysteinesulfinate in rat liver mitochondria was studied. Incubation of 10 mMl-cysteine with rat liver mitochondria at 37°C in the presence of 10 mM 2-oxoglutarate and 10 mM glutathione resulted in the formation of 4.60 and 1.52µmol of sulfate and thiosulfate, respectively, per 60 min per mitochondria obtained from 1 g of liver. Under the same conditions sulfate formation froml-cysteinesulfinate was 24.96µmol, but thiosulfate was not formed. The addition of (aminooxy)acetate at 2 mM or more completely inhibited the sulfate and thiosulfate formation froml-cysteine and the sulfate formation froml-cysteinesulfinate. These findings support our previous conclusion that cysteine transamination and 3-mercaptopyruvate pathway (MP pathway) are involved in the sulfate formation froml-cysteine in rat liver mitochondria (Ubuka et al., 1992).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00805987
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Metabolism ofl-cysteine via transamination pathway (3-mercaptopyruvate pathway) (1992)
    Springer
    Amino acids 3 (1992), S. 243-252 
    Details
    ISSN: 1438-2199
    Keywords: Amino acids ; Cysteine metabolism ; 3-Mercaptopyruvate pathway ; Cysteine transamination ; 3-Mercaptolactate-cysteine mixed disulfide ; Sulfate formation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We have studied the transamination pathway (3-mercaptopyruvate pathway) ofl-cysteine metabolism in rats. Characterization of cysteine aminotransferase (EC 2.6.1.3) from liver indicated that the transamination, the first reaction of this pathway, was catalyzed by aspartate aminotransferase (EC 2.6.1.1). 3-Mercaptopyruvate, the product of the transamination, may be metabolized through two routes. The initial reactions of these routes are reduction and transsulfuration, and the final metabolites are 3-mercaptolactate-cysteine mixed disulfide [S-(2-hydroxy-2-carboxyethylthio)cysteine, HCETC] and inorganic sulfate, respectively. The study using anti-lactate dehydrogenase antiserum proved that the enzyme catalyzing the reduction of 3-mercaptopyruvate was lactate dehydrogenase (EC 1.1.1.27). Formation of HCETC was shown to depend on low 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) activity. Results were discussed in relation to HCETC excretion in normal human subjects and patients with 3-mercaptolactate-cysteine disulfiduria. Incubation of liver mitochondria withl-cysteine, 2-oxoglutarate and glutathione resulted in the formation of sulfate and thiosulfate, indicating that thiosulfate was formed by transsulfuration of 3-mercaptopyruvate and finally metabolized to sulfate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00805999
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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