Document Detail


On the interpretation of tyrosinase inhibition kinetics.
MedLine Citation:
PMID:  23323989     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Abstract Tyrosinases (monophenol monooxygenases, EC 1.14.18.1) utilize a reaction mechanism that involves two intertwined catalytic cycles and at least three different ligand-binding enzyme forms. Therefore a variety of different inhibition types may arise in inhibition experiments, depending on the binding mode of the compound studied. Here we discuss a steady-state equation that describes inhibition of the diphenolase cycle of tyrosinase catalysis in a general way. In addition, we employ numerical simulations to explore the kinetic outcome of various binding schemes. As the full equation is far too complex to be applicable for data evaluation by curve fitting, we propose to use the general modifier scheme of Botts-Morales for fitting and demonstrate that especially the value of parameter α of the equation allows conclusions about the binding mode of the inhibitor. The approach is exemplified by selected data describing the inhibition of human tyrosinase by typical inhibitors.
Authors:
Wei Sun; Michael Wendt; Gerhard Klebe; Klaus-Heinrich Röhm
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-17
Journal Detail:
Title:  Journal of enzyme inhibition and medicinal chemistry     Volume:  -     ISSN:  1475-6374     ISO Abbreviation:  J Enzyme Inhib Med Chem     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-17     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101150203     Medline TA:  J Enzyme Inhib Med Chem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Institute of Pharmaceutical Chemistry and.
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