Mammalian tyrosinase; action on substances structurally related to tyrosine.

نویسندگان

  • A B LERNER
  • T B FITZPATRICK
  • E CALKINS
  • W H SUMMERSON
چکیده

Tyrosinase prepared from plant, insect, and marine animal sources catalyzes the oxidation of tyrosine, dihydroxyphenylalanine (dopa), and various structurally similar compounds to darkly colored pigments (2). The enzymatic oxidation of many of the analogues of tyrosine and dopa often proceeds at a faster rate than for tyrosine and dopa themselves (2, 3). The investigation reported here was carried out in order to determine the action of tyrosinase from mammalian sources on various compounds structurally related to tyrosine and dopa so that information regarding the mechanism of mammalian tyrosinase action might be obtained. The possibility of finding competitive inhibitors for mammalian tyrosinase action was also anticipated.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Peroxidase, "protyrosinase," and the multiple forms of tyrosinase in mice.

Mammalian tyrosinase as currently defined has two catalytic functions: 1) the oxidation of tyrosine to L-3,4-dihydroxyphenylalanine (dopa) and 2) the oxidation of dopa to dopa quinone (1-9). Although an imposing body of evidence has been advanced in support of this interpretation, Okun and associates have recently challenged the prevailing concept of the action of tyrosinase ( 10, 11 ). They ha...

متن کامل

Histochemical evidence that peroxidase does not affect melanin formation in feather melanocytes.

Animal peroxidases are iron-containing proteins that catalyze the oxidation of a variety of substances by hydrogen peroxide. Histochemically, the myeloperoxidase of granulocytes is the most easily detected (1). Tyrosinase (dopa oxidase) is a copper-containing enzyme complex capable of converting both tyrosine to dopa (slowly) and dopa to dopa quinone (rapidly) in the melanin synthetic pathway (...

متن کامل

Mutational mapping of the catalytic activities of human tyrosinase.

Tyrosinase (EC 1.14.18.1) is a copper-containing metalloglycoprotein that catalyzes several steps in the melanin pigment biosynthetic pathway; the hydroxylation of tyrosine to L-3,4-dihydroxyphenylalanine (dopa) and the subsequent oxidation of dopa to dopaquinone. It has been proposed that tyrosinase is also able to oxidize 5,6-dihydroxyindole (DHI), a later product in the melanogenic pathway, ...

متن کامل

A revised concept of mammalian melanogenesis: the possible synergistic functions of aerobic dopa oxidase and peroxidase. A review.

The enzymatic oxidation of tyrosine to melanin in mammalian cells is widely believed to be mediated solely by an aerobic, copper-dependent enzyme called tyrosinase (1). This enzyme is considered to be analogous to the tyrosinase of plants and insects, which has been shown to mediate the first two steps of the tyrosine to melanin sequence (2-4): hydroxylation of tyrosine to dopa and oxidation of...

متن کامل

A second tyrosinase-related protein, TRP-2, is a melanogenic enzyme termed DOPAchrome tautomerase.

The production of melanin pigment in mammals requires tyrosinase, an enzyme which hydroxylates the amino acid tyrosine to DOPA (3,4-dihydroxyphenylalanine), thus allowing the cascade of reactions necessary to synthesize that biopolymer. However, there are other regulatory steps that follow the action of tyrosinase and modulate the quantity and quality of the melanin produced. DOPAchrome tautome...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 191 2  شماره 

صفحات  -

تاریخ انتشار 1951