Document Detail

Kinetic cooperativity of tyrosinase. A general mechanism.
MedLine Citation:
PMID:  21887411     Owner:  NLM     Status:  Publisher    
Tyrosinase shows kinetic cooperativity in its action on o-diphenols, but not when it acts on monophenols, confirming that the slow step is the hydroxylation of monophenols to o-diphenols. This model can be generalised to a wide range of substrates; for example, type S(A) substrates, which give rise to a stable product as the o-quinone evolves by means of a first or pseudo first order reaction (α-methyl-Dopa, Dopa methyl ester, dopamine, 3,4-dihydroxyphenylpropionic acid, 3,4-dihydroxyphenylacetic acid, α-methyl-tyrosine, tyrosine methyl ester, tyramine, 4-hydroxyphenylpropionic acid and 4-hydroxyphenylacetic acid), type S(B) substrates, which include those whose o-quinone evolves with no clear stoichiometry (catechol, 4-methylcatechol, phenol and p-cresol) and, lastly, type S(C) substrates, which give rise to stable o-quinones (4-tert-butylcatechol/4-tert-butylphenol).
Jose Luis Muñoz-Muñozd; Francisco Garcia-Molinad; Ramón Varond; Jose Tudelad; Francisco Garcia-Cánovasd; Jose N Rodríguez-Lópezd
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-8-29
Journal Detail:
Title:  Acta biochimica Polonica     Volume:  -     ISSN:  1734-154X     ISO Abbreviation:  -     Publication Date:  2011 Aug 
Date Detail:
Created Date:  2011-9-2     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  14520300R     Medline TA:  Acta Biochim Pol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
GENZ: Grupo de Investigación Enzimología, Departamento de Bioquímica y Biología Molecular-A, Facultad de Biología, Universidad de Murcia, Espinardo, Murcia, Spain.
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