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. 1992 Oct;20(2):245-53.
doi: 10.1007/BF00014492.

Cloning and characterization of cDNAs coding for Vicia faba polyphenol oxidase

J W Cary  1 , A R Lax, W H Flurkey
Affiliations

Cloning and characterization of cDNAs coding for Vicia faba polyphenol oxidase

J W Cary et al. Plant Mol Biol. 1992 Oct.

Abstract

Three cDNA clones were isolated which code for the ubiquitous chloroplast enzyme, polyphenol oxidase (PPO), from Vicia faba. Analysis of the cloned DNA reveals that PPO is synthesized with an N-terminal extension of 92 amino acid residues, presumed to be a transit peptide. The mature protein is predicted to have a molecular mass of 58 kDa which is in close agreement to the molecular mass estimated for the in vivo protein upon SDS-PAGE. Differences in the DNA sequence of two full-length and one partial cDNA clones indicate that PPO is encoded by a gene family. Analysis of the deduced amino acid sequence shows that the chloroplast PPO shares homology with the 59 kDa PPOs in glandular trichomes of solanaceous species. A high degree of sequence conservation was found with the copper-binding domains of the 59 kDa tomato PPO as well as hemocyanins and tyrosinases from a wide diversity of taxa.

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