- Tytuł:
- Kinetic cooperativity of tyrosinase. A general mechanism
- Autorzy:
-
Muñoz-Muñoz, Jose
Garcia-Molina, Francisco
Varon, Ramón
Tudela, Jose
Garcia-Cánovas, Francisco
Rodríguez-López, Jose - Powiązania:
- https://bibliotekanauki.pl/articles/1039877.pdf
- Data publikacji:
- 2011
- Wydawca:
- Polskie Towarzystwo Biochemiczne
- Tematy:
-
o-diphenols
tyrosinase - Opis:
- 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).
- Źródło:
-
Acta Biochimica Polonica; 2011, 58, 3; 303-311
0001-527X - Pojawia się w:
- Acta Biochimica Polonica
- Dostawca treści:
- Biblioteka Nauki
Artykuł