| Kinetic cooperativity of tyrosinase. A general mechanism. | |
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MedLine Citation:
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PMID: 21887411 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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). |
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Authors:
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Jose Luis Muñoz-Muñozd; Francisco Garcia-Molinad; Ramón Varond; Jose Tudelad; Francisco Garcia-Cánovasd; Jose N Rodríguez-Lópezd |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-8-29 |
Journal Detail:
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Title: Acta biochimica Polonica Volume: - ISSN: 1734-154X ISO Abbreviation: - Publication Date: 2011 Aug |
Date Detail:
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Created Date: 2011-9-2 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 14520300R Medline TA: Acta Biochim Pol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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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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