PMID: 8610068Aug 1, 1995Paper

Complex formation between mushroom tyrosinase and Manduca dopachrome isomerase

Pigment Cell Research
M SugumaranC Amaratunga

Abstract

Melanin biosynthesis in animals is initiated by the ubiquitously present tyrosinase and is aided by dopachrome isomerase. We have characterized a novel dopachrome isomerase (decarboxylating) from the hemolymph of Manduca sexta that generates a new quinone methide intermediate during melanogenesis (Sugumaran, M. and Semensi, V. (1991) J. Biol. Chem. 266, 6073-6078). This enzyme has the ability to form a complex with mushroom tyrosinase as judged by a number of physicochemical studies. The isomerase exhibited a marked inhibitory effect on tyrosinase and tyrosinase reciprocated by inhibiting the isomerase. While the isomerase showed no activity toward preformed dopaminechrome, it readily influenced the stability of dopaminechrome generated in situ by tyrosinase. Moreover, mushroom tyrosinase, which lacked specific binding to Concanavalin A Sepharose column, after complexing with the isomerase exhibited binding to this column. The complex formation also affected the pI value as well as mobility on a size exclusion column of these enzymes. Enzymes executing sequential metabolic transformation are known to form complexes called metabolons. Based on these above studies, it is concluded that both the enzymes involved in insect melanoge...Continue Reading

References

Nov 1, 1992·Pigment Cell Research·M Sugumaran
Jan 1, 1991·Chemico-biological Interactions·P J O'Brien
Mar 1, 1991·Pigment Cell Research·J M Pawelek
Feb 14, 1990·Biochemical and Biophysical Research Communications·J M Pawelek
Aug 1, 1980·The Journal of Investigative Dermatology·A M Körner, J Pawelek

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Citations

Nov 11, 1999·Biotechnic & Histochemistry : Official Publication of the Biological Stain Commission·K Valivittan
Jul 19, 2000·Archives of Biochemistry and Biophysics·M SugumaranK Valivittan

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