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Molecular basis of substrate and inhibitory specificity of tyrosinase: phenolic compounds
Author(s) -
PASSI S.,
NAZZAROPORRO M.
Publication year - 1981
Publication title -
british journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.304
H-Index - 179
eISSN - 1365-2133
pISSN - 0007-0963
DOI - 10.1111/j.1365-2133.1981.tb00752.x
Subject(s) - tyrosinase , chemistry , substrate (aquarium) , in vivo , inhibitory postsynaptic potential , in vitro , combinatorial chemistry , non competitive inhibition , molecule , biochemistry , enzyme , stereochemistry , organic chemistry , biology , microbiology and biotechnology , ecology , neuroscience
SUMMARY In order to investigate the molecular basis of substrates, and the inhibitory specificity of tyrosinase, a large series of phenolic compounds have been analysed by using a High Performance Liquid Chromatographic‐Scanning Spectrophotometric system. Depending on their chemical structure, phenolic compounds may act as substrates or as competitive inhibitors of tyrosinase. The ability to act as substrates requires the presence in the molecule of electron donor groups, while competitive inhibition on the contrary requires the presence of powerful electron acceptor groups. Certain phenolic compounds used as therapeutic agents or as food preservatives are chemically capable of acting as alternative substrates or competitive inhibitors of tyrosinase in vitro ; their effect on melanocytes in vivo therefore merits investigation.