Structural diversity in the dandelion (Taraxacum officinale) polyphenol oxidase family results in different responses to model substrates.

Polyphenol oxidases (PPOs) are ubiquitous type-3 copper enzymes that catalyze the oxygen-dependent conversion of o-diphenols to the corresponding quinones. In most plants, PPOs are present as multiple isoenzymes that probably serve distinct functions, although the precise relationship between sequen...

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Autores principales:	Mareike E Dirks-Hofmeister, Ratna Singh, Christine M Leufken, Jennifer K Inlow, Bruno M Moerschbacher
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ea79f2d779e44238b617205647c13dfa
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spelling	oai:doaj.org-article:ea79f2d779e44238b617205647c13dfa2021-11-18T08:16:06ZStructural diversity in the dandelion (Taraxacum officinale) polyphenol oxidase family results in different responses to model substrates.1932-620310.1371/journal.pone.0099759https://doaj.org/article/ea79f2d779e44238b617205647c13dfa2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24918587/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Polyphenol oxidases (PPOs) are ubiquitous type-3 copper enzymes that catalyze the oxygen-dependent conversion of o-diphenols to the corresponding quinones. In most plants, PPOs are present as multiple isoenzymes that probably serve distinct functions, although the precise relationship between sequence, structure and function has not been addressed in detail. We therefore compared the characteristics and activities of recombinant dandelion PPOs to gain insight into the structure-function relationships within the plant PPO family. Phylogenetic analysis resolved the 11 isoenzymes of dandelion into two evolutionary groups. More detailed in silico and in vitro analyses of four representative PPOs covering both phylogenetic groups were performed. Molecular modeling and docking predicted differences in enzyme-substrate interactions, providing a structure-based explanation for grouping. One amino acid side chain positioned at the entrance to the active site (position HB2+1) potentially acts as a "selector" for substrate binding. In vitro activity measurements with the recombinant, purified enzymes also revealed group-specific differences in kinetic parameters when the selected PPOs were presented with five model substrates. The combination of our enzyme kinetic measurements and the in silico docking studies therefore indicate that the physiological functions of individual PPOs might be defined by their specific interactions with different natural substrates.Mareike E Dirks-HofmeisterRatna SinghChristine M LeufkenJennifer K InlowBruno M MoerschbacherPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 6, p e99759 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Mareike E Dirks-Hofmeister Ratna Singh Christine M Leufken Jennifer K Inlow Bruno M Moerschbacher Structural diversity in the dandelion (Taraxacum officinale) polyphenol oxidase family results in different responses to model substrates.
description	Polyphenol oxidases (PPOs) are ubiquitous type-3 copper enzymes that catalyze the oxygen-dependent conversion of o-diphenols to the corresponding quinones. In most plants, PPOs are present as multiple isoenzymes that probably serve distinct functions, although the precise relationship between sequence, structure and function has not been addressed in detail. We therefore compared the characteristics and activities of recombinant dandelion PPOs to gain insight into the structure-function relationships within the plant PPO family. Phylogenetic analysis resolved the 11 isoenzymes of dandelion into two evolutionary groups. More detailed in silico and in vitro analyses of four representative PPOs covering both phylogenetic groups were performed. Molecular modeling and docking predicted differences in enzyme-substrate interactions, providing a structure-based explanation for grouping. One amino acid side chain positioned at the entrance to the active site (position HB2+1) potentially acts as a "selector" for substrate binding. In vitro activity measurements with the recombinant, purified enzymes also revealed group-specific differences in kinetic parameters when the selected PPOs were presented with five model substrates. The combination of our enzyme kinetic measurements and the in silico docking studies therefore indicate that the physiological functions of individual PPOs might be defined by their specific interactions with different natural substrates.
format	article
author	Mareike E Dirks-Hofmeister Ratna Singh Christine M Leufken Jennifer K Inlow Bruno M Moerschbacher
author_facet	Mareike E Dirks-Hofmeister Ratna Singh Christine M Leufken Jennifer K Inlow Bruno M Moerschbacher
author_sort	Mareike E Dirks-Hofmeister
title	Structural diversity in the dandelion (Taraxacum officinale) polyphenol oxidase family results in different responses to model substrates.
title_short	Structural diversity in the dandelion (Taraxacum officinale) polyphenol oxidase family results in different responses to model substrates.
title_full	Structural diversity in the dandelion (Taraxacum officinale) polyphenol oxidase family results in different responses to model substrates.
title_fullStr	Structural diversity in the dandelion (Taraxacum officinale) polyphenol oxidase family results in different responses to model substrates.
title_full_unstemmed	Structural diversity in the dandelion (Taraxacum officinale) polyphenol oxidase family results in different responses to model substrates.
title_sort	structural diversity in the dandelion (taraxacum officinale) polyphenol oxidase family results in different responses to model substrates.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/ea79f2d779e44238b617205647c13dfa
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Structural diversity in the dandelion (Taraxacum officinale) polyphenol oxidase family results in different responses to model substrates.

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