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茴香酸的酪氨酸酶抑制动力学

Tyrosinase inhibition kinetics of anisic acid.

作者信息

Kubo Isao, Chen Qing-Xi, Nihei Ken-Ichi, Calderón José S, Céspedes Carlos L

机构信息

Department of Environmental Science, Policy and Management, University of California, Berkeley, California 94720-3112, USA.

出版信息

Z Naturforsch C J Biosci. 2003 Sep-Oct;58(9-10):713-8. doi: 10.1515/znc-2003-9-1021.

DOI:10.1515/znc-2003-9-1021
PMID:14577637
Abstract

Anisic acid (p-methoxybenzoic acid) was characterized as a tyrosinase inhibitor from ani-seed, a common food spice. It inhibited the oxidation of L-3,4-dihydroxyphenylalanine (L-DOPA) catalyzed by tyrosinase with an IC50 of 0.60 mM. The inhibition of tyrosinase by anisic acid is a reversible reaction with residual enzyme activity. This phenolic acid was found to be a classical noncompetitive inhibitor and the inhibition constant K(I) was obtained as 0.603 mM. Anisic acid also inhibited the hydroxylation of L-tyrosine catalyzed by tyrosinase. The lag phase caused by the monophenolase activity was lengthened and the steady-state activity of the enzyme was decreased by anisic acid.

摘要

茴香酸(对甲氧基苯甲酸)被鉴定为一种来自常见食用香料茴芹籽的酪氨酸酶抑制剂。它抑制酪氨酸酶催化的L - 3,4 - 二羟基苯丙氨酸(L - DOPA)氧化,IC50为0.60 mM。茴香酸对酪氨酸酶的抑制是一种具有残余酶活性的可逆反应。这种酚酸被发现是一种典型的非竞争性抑制剂,抑制常数K(I)为0.603 mM。茴香酸还抑制酪氨酸酶催化的L - 酪氨酸羟基化。茴香酸延长了由单酚酶活性引起的延迟期,并降低了该酶的稳态活性。

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