(mŏn′ō-fē′nôl′, -nōl′)
A compound containing one phenolic hydroxyl group.
The American Heritage® Medical Dictionary Copyright © 2007, 2004 by Houghton Mifflin Company. Published by Houghton Mifflin Company. All rights reserved.
References in periodicals archive ?
Tyrosinases (sometimes referred to as polyphenol oxidases, monophenol monoxygenases, catechol oxidases, cre-solases, or catecholases) are well known for their role in producing melanin in vertebrates.
monophenol monooxygenase, polyphenoloxidase, catechol oxidase, and oxidoreductase), a copper-containing enzyme that induces formation of catecholamine quinone derivatives by its oxidase activity, makes a point since it has been demonstrated to cause a neuronal toxicity through oxidation of cytosolic excess dopamine in PD [9].
Tyrosinase (EC, a coppercontaining enzyme that is crucial for melanin production [29], oxidizes monophenol (tyrosine) to odiphenol L-DOPA and subsequently to o-quinone dopachrome, which then undergoes chemical and enzymatic reactions to yield melanin [30].
Tyrosinase (monophenol dihydroxyphenyl alanine; EC is a copper containing metallo enzyme which catalyzes the oxidation of phenols, the ortho hydroxylation of monophenols to Odiphenols (monophenolase activity), and the oxidation of Oquinones (diphenolase activity).
PO possesses both monophenol monooxygenase activity (EC, tyrosine, dihydroxyphenylalanine, oxygen, and oxidoreductase) and o-diphenoloxidase activity (EC, o-diphenol, oxygen, and oxidoreductase) [7, 8].
The monophenol nature of betanin and reducing intermediates during the oxidation process may confer to the molecule a higher H-atom or electron donation potential.
It can catalyze 2 reactions through hydroxylation of monophenol to o-diphenol and by oxidation of o-diphenol into the corresponding o-quinone [8].
Tudela, "Tyrosinase kinetics: discrimination between two models to explain the oxidation mechanism of monophenol and diphenol substrates," The International Journal of Biochemistry & Cell Biology, vol.
The construction of an IQA producing bacterial platform therefore requires the use of Ralstonia solanacearum tyrosinase (TYR; EC, monophenol, L-DOPA: oxygen oxidoreductase) to produce L-DOPA from L-tyrosine.
The manufacturing process of the lignophenol developed by Funaoka (47), (48) is generally called "the phase-separation conversion method." Some monophenol derivatives including [rho]-cresol are applicable to the conversion method.
This oxidase catalyzes two distinct reactions of melanin synthesis, the hydroxylation of a monophenol and the conversion of an o-diphenol to the corresponding oquinone [12].
Tyrosinase (monophenol, polyphenol oxidase; EC catalyzes the hydroxylation of L-tyrosine to 3,4-dihydroxyphenyalalanine (L-DOPA) and the subsequent oxidation of L-DOPA to dopaquinone (Fenoll et al., 2002).