Cytosolic Mercaptopyruvate Sulfurtransferase Is Evolutionarily Related to Mitochondrial Rhodanese.
نویسندگان
چکیده
منابع مشابه
Expression of 3-Mercaptopyruvate Sulfurtransferase in the Mouse.
3-Mercaptopyruvate sulfurtransferase (MST) is one of the principal enzymes for the production of hydrogen sulfide and polysulfides in mammalians, and emerging evidence supports the physiological significance of MST. As a fundamental study of the physiology and pathobiology of MST, it is necessary to establish the tissue distribution of MST in mice. In the present study, the expression of MST in...
متن کاملFunctional Analysis of 3-Mercaptopyruvate Sulfurtransferase Using Knockout Mice
3-mercaptopyruvate sulfurtransferase (MST) is a universal enzyme in prokaryotes and eukaryotes. In 1998, we reported the distribution of MST in rat [1]. MST was expressed in numerous somatic cells and was found to be present in both cytosol and mitochondria [1] (Figure 1a). In the kidney, MST levels were higher in the cortex and proximal convoluted tubules as compared to that in the medulla and...
متن کاملThe mercaptopyruvate sulfurtransferase of Trichomonas vaginalis links cysteine catabolism to the production of thioredoxin persulfide.
Trichomonas vaginalis is a protozoan parasite of humans that is able to synthesize cysteine de novo using cysteine synthase but does not produce glutathione. In this study, high pressure liquid chromatography analysis confirmed that cysteine is the major intracellular redox buffer by showing that T. vaginalis contains high levels of cysteine ( approximately 600 mum) comprising more than 70% of ...
متن کاملThioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide.
H2S (hydrogen sulfide) has recently been recognized as a signalling molecule as well as a cytoprotectant. We recently demonstrated that 3MST (3-mercaptopyruvate sulfurtransferase) produces H2S from 3MP (3-mercaptopyruvate). Although a reducing substance is required for an intermediate persulfide at the active site of 3MST to release H2S, the substance has not been identified. In the present stu...
متن کاملIs development of high-grade gliomas sulfur-dependent?
We characterized γ-cystathionase, rhodanese and 3-mercaptopyruvate sulfurtransferase activities in various regions of human brain (the cortex, thalamus, hypothalamus, hippocampus, cerebellum and subcortical nuclei) and human gliomas with II to IV grade of malignancy (according to the WHO classification). The human brain regions, as compared to human liver, showed low γ-cystathionase activity. T...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1074/jbc.270.27.16230