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Subcellular Compartmentation and Biological Functions of Mercaptopyruvate Sulphurtransferase and Rhodanese

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Abstract

According to present knowledge transfer of bivalent or sulphane sulphur from thiosulphate, thiocystine, 3-mercaptopyruvate and some other donors is catalyzed by at least three different enzymes: rhodanese /EC 2.8. 1.1/, thiosulphate reductase /no EC number/ and mercapto-pyruvate sulphurtransferase /EC 2.8.1.2/ /for references see Westley, 1973; Koj et al.,1975/. The mechanism of their action is not uniform: rhodanese operates by a double-displacement mechanism /cf. Westley, 1973/ mercaptopyruvate sulphurtransferase by a sequential reaction /Jarabak and Westley,1978/, while the mode of action of thiosulphate reductase is not elucidated.

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© 1980 Plenum Press, New York

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Koj, A. (1980). Subcellular Compartmentation and Biological Functions of Mercaptopyruvate Sulphurtransferase and Rhodanese. In: Cavallini, D., Gaull, G.E., Zappia, V. (eds) Natural Sulfur Compounds. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-3045-5_45

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  • DOI: https://doi.org/10.1007/978-1-4613-3045-5_45

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-3047-9

  • Online ISBN: 978-1-4613-3045-5

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