Production of 6-hydroxydopa by human tyrosinase.

Abstract

A tyrosinase obtained from cultured human melanoma cells was found to oxygenate 2,4-dihydroxyphenylalanine to the strongly cytotoxic amino acid 6-hydroxydopa (2,4,5-trihydroxyphenylalanine). The oxygenation was dependent on the presence of a reducing co-substrate such as dopa or dopamine. The rate of oxygenation of 2,4-dihydroxyphenyl-D,L-alanine was similar to that of L-tyrosine, the normal substrate of tyrosinase. The enzymatic reaction demonstrated may prove of value in the chemotherapy of human melanoma.

• Authors: C Hansson, H Rorsman, E Rosengren, A Wittbjer
• Journal: Acta dermato-venereologica (Acta Derm Venereol) Vol. 65 Issue 2 Pg. 154-7 ( 1985) ISSN: 0001-5555 [Print] Sweden
• PMID: 2408419 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Culture Media
• 6-hydroxydopa
• Dihydroxyphenylalanine
• Catechol Oxidase
• Monophenol Monooxygenase

Topics

• Catalysis
• Catechol Oxidase (metabolism)
• Cell Line
• Culture Media
• Dihydroxyphenylalanine (analogs & derivatives, biosynthesis, metabolism)
• Humans
• Melanoma
• Monophenol Monooxygenase (metabolism)