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J Inorg Biochem. 2008 Dec;102(12):2160-70. doi: 10.1016/j.jinorgbio.2008.08.007. Epub 2008 Aug 30.

Proteolytic processing of polyphenol oxidase from plants and fungi.

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  • 1Department of Chemistry, Indiana State University, Terre Haute, IN 47809, USA.

Abstract

Polyphenol oxidase (PPO), a metalloenzyme containing a type-3 copper center, is produced by many species of plants, fungi, and bacteria. There is great variability in the subunit molecular mass reported for PPO, even from a single species. In some cases, experimental evidence (usually protein sequencing by Edman degradation) indicates that the variability in molecular mass for PPO from a given species is the result of proteolytic processing at the N and/or C-termini of the protein. In order to identify specific sequence regions where proteolysis occurs in PPO from most species, the experimentally established N and C-termini of these proteolyzed enzymes were compared to the protein sequences of other PPOs for which the N and C-termini have not been established by protein sequencing methods. In all cases the N-terminal proteolysis sites were located prior to a conserved arginine residue, and the C-terminal proteolysis sites were located following a conserved tyrosine motif. Based on the sites of proteolysis, molecular masses were calculated for the enzymes, and the calculated values were used to rationalize the varying molecular masses reported in the literature. To determine the structural implications of N and C-terminal proteolysis, the proteolysis sites were related to the two available PPO structures: Ipomoea batatas catechol oxidase and Streptomyces castaneoglobisporus tyrosinase. A structural "core" region that appears to be essential for structural stability and enzymatic activity was identified.

PMID:
18829115
[PubMed - indexed for MEDLINE]
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