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Article

In crystallo activity tests with latent apple tyrosinase and two mutants reveal the importance of the mutated sites for polyphenol oxidase activity.

Acta crystallographica. Section F, Structural biology communications - 1 Aug 2017

Kampatsikas Ioannis, Bijelic Aleksandar, Pretzler Matthias, Rompel Annette

Abstract excerpt

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 (MdPPO1) was recombinantly expressed in its latent form (56.4 kDa) and...

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Identifiers

PMID: 28777094
DOI: 10.1107/S2053230X17010822
PMCID: PMC5544008

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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