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• W2740369441 endingPage "499" @default.
• W2740369441 startingPage "491" @default.
• W2740369441 abstract "Tyrosinases are type 3 copper enzymes that belong to the polyphenol oxidase (PPO) family and are able to catalyze both the ortho -hydroxylation of monophenols and their subsequent oxidation to o -quinones, which are precursors for the biosynthesis of colouring substances such as melanin. The first plant pro-tyrosinase from Malus domestica ( Md PPO1) was recombinantly expressed in its latent form (56.4 kDa) and mutated at four positions around the catalytic pocket which are believed to influence the activity of the enzyme. Mutating the amino acids, which are known as activity controllers, yielded the mutants Md PPO1-Ala239Thr and Md PPO1-Leu243Arg, whereas mutation of the so-called water-keeper and gatekeeper residues resulted in the mutants Md PPO1-Glu234Ala and Md PPO1-Phe259Ala, respectively. The wild-type enzyme and two of the mutants, Md PPO1-Ala239Thr and Md PPO1-Phe259Ala, were successfully crystallized, leading to single crystals that diffracted to 1.35, 1.55 and 1.70 Å resolution, respectively. All crystals belonged to space group P 2 1 2 1 2 1 , exhibiting similar unit-cell parameters: a = 50.70, b = 80.15, c = 115.96 Å for the wild type, a = 50.58, b = 79.90, c = 115.76 Å for Md PPO1-Ala239Thr and a = 50.53, b = 79.76, c = 116.07 Å for Md PPO1-Phe259Ala. In crystallo activity tests with the crystals of the wild type and the two mutants were performed by adding the monophenolic substrate tyramine and the diphenolic substrate dopamine to crystal-containing drops. The effects of the mutation on the activity of the enzyme were observed by colour changes of the crystals owing to the conversion of the substrates to dark chromophore products." @default.
• W2740369441 created "2017-08-08" @default.
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• W2740369441 date "2017-07-28" @default.
• W2740369441 modified "2023-10-17" @default.
• W2740369441 title "<i>In crystallo</i>activity tests with latent apple tyrosinase and two mutants reveal the importance of the mutated sites for polyphenol oxidase activity" @default.
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• W2740369441 doi "https://doi.org/10.1107/s2053230x17010822" @default.
• W2740369441 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5544008" @default.
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