Kinetic cooperativity of tyrosinase. A general mechanism

• Autorzy: Munoz-Munoz J. L. , Garcia-Molina F. , Varon R. , Tudela J. , Garcia-Canovas F. , Rodriguez-Lopez J. N.
• Języki publikacji: EN

Abstrakty

EN

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 SA 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 SB substrates, which include those whose o-quinone evolves with no clear stoichiometry (catechol, 4-methylcatechol, phenol and p-cresol) and, lastly, type SC substrates, which give rise to stable o-quinones (4-tert-butylcatechol/4-tert-butylphenol).

Słowa kluczowe

EN

tyrosinase; o-diphenol; monophenol; hydroxylation; monophenolase activity; diphenolase activity

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2011
• Tom: 58
• Numer: 3
• Opis fizyczny: p.

Twórcy

autor

Munoz-Munoz J. L.

• GENZ: Grupo de Investigacion Enzimologia, Departamento de Bioquimica y Biologia Molecular-A, Facultad de Biología, Universidad de Murcia, Espinardo, Murcia, Spain

autor

Garcia-Molina F.

autor

Varon R.

autor

Tudela J.

autor

Garcia-Canovas F.

autor

Rodriguez-Lopez J. N.

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