@article{ref1,
title="Tyrosinase inactivation in its action on dopa",
journal="Biochimica et biophysica acta",
year="2010",
author="Muñoz-Muñoz, J. L. and Acosta-Motos, J. R. and García-Molina, F. and Varon, R. and Garcia-Ruíz, P. A. and Tudela, J. and García-Cánovas, F. and Rodríguez-López, J. N.",
volume="1804",
number="7",
pages="1467-1475",
abstract="Under aerobic or anaerobic conditions, tyrosinase undergoes a process of irreversible inactivation induced by its physiological substrate L-dopa. Under aerobic conditions, this inactivation occurs through a process of suicide inactivation involving the form oxy-tyrosinase. Under anaerobic conditions, both the met- and deoxy-tyrosinase forms undergo irreversible inactivation. Suicide inactivation in aerobic conditions is slower than the irreversible inactivation under anaerobic conditions. The enzyme has less affinity for the isomer D-dopa than for L-dopa but the velocity of inactivation is the same. We propose mechanisms to explain these processes.<p /><p>Language: en</p>",
language="en",
issn="0006-3002",
doi="10.1016/j.bbapap.2010.02.015",
url="http://dx.doi.org/10.1016/j.bbapap.2010.02.015"
}