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Front Cover: Similar but Still Different: Which Amino Acid Residues Are Responsible for Varying Activities in Type‐III Copper Enzymes? (7/2021)
Author(s) -
Kampatsikas Ioannis,
Rompel Annette
Publication year - 2021
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202100114
Subject(s) - copper , catechol oxidase , amino acid , enzyme , chemistry , front cover , catechol , browning , substrate (aquarium) , tyrosinase , biochemistry , stereochemistry , polyphenol oxidase , organic chemistry , cover (algebra) , biology , ecology , mechanical engineering , peroxidase , engineering
Type‐III copper proteins are ubiquitous among organisms and catalyze the transfer and activation of molecular oxygen. Tyrosinases hydroxylate monophenols and oxidize the corresponding diphenols, whereas catechol oxidases have only the latter activity. The substrate preference of the two subgroups is controlled by amino acids around the two copper ions, which guide the similar type‐III copper centers into different catalytic pathways. The produced quinones polymerize to melanins, resulting in the browning of fruits and human skin, hair, and eye color. More information can be found in the minireview by I. Kampatsikas and A. Rompel et al.