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Polyphenol oxidase is an enzyme found throughout the plant and animal kingdoms, [31] including most fruits and vegetables. [32] PPO has importance to the food industry because it catalyzes enzymatic browning when tissue is damaged from bruising, compression or indentations, making the produce less marketable and causing economic loss.
Peroxidase activity is measured by running the phenol oxidase assay concurrently with another assay with L-DOPA and hydrogen peroxide (H 2 O 2) added to every sample. [48] The difference in measurements between the two assays is indicative of peroxidase activity. Enzyme assays typically apply proxies that reveal exo-acting activities of enzymes.
Oxidopamine, also known as 6-hydroxydopamine (6-OHDA) or 2,4,5-trihydroxyphenethylamine, is a synthetic monoaminergic neurotoxin used by researchers to selectively destroy dopaminergic and noradrenergic neurons in the brain.
l-DOPA, also known as l-3,4-dihydroxyphenylalanine and used medically as levodopa, is made and used as part of the normal biology of some plants [2] and animals, including humans. Humans, as well as a portion of the other animals that utilize l -DOPA, make it via biosynthesis from the amino acid l -tyrosine .
Ceruloplasmin EC 1.16.3.1 (ferroxidase), a 6-domain enzyme found in the serum of mammals and birds that oxidizes different inorganic and organic substances; exhibits internal sequence homology that appears to have evolved from the triplication of a Cu-binding domain similar to that of laccase and ascorbate oxidase. Laccase EC 1.10.3.2 (urishiol ...
Tyrosine hydroxylase or tyrosine 3-monooxygenase is the enzyme responsible for catalyzing the conversion of the amino acid L-tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA). [5] [6] It does so using molecular oxygen (O 2), as well as iron (Fe 2+) and tetrahydrobiopterin as cofactors.
3,4-Dihydroxyphenylacetic acid (DOPAC) is a metabolite of the neurotransmitter dopamine.Dopamine can be metabolized into one of three substances. One such substance is DOPAC.
Proteins in the oothecal foam of the mantis are cross-linked covalently by small molecules related to L-DOPA via a tanning reaction that is catalysed by catechol oxidase or polyphenol oxidase enzymes. [citation needed] L-DOPA is a tyrosine residue that bears an additional hydroxyl group.