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...
Topics
- Amino Acid Sequence
- Amino Acid Substitution
- Binding Sites
- Cloning, Molecular
- Copper
- Crystallography, X-Ray
- Dopamine
- Escherichia coli
- Gene Expression
- Genetic Vectors
- Hydroxylation
- Malus
- Models, Molecular