Structure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A4

Abstract Enzymatic conversion of chitin, a β-1,4 linked polymer of N-acetylglucosamine, is of major interest in areas varying from the biorefining of chitin-rich waste streams to understanding how medically relevant fungi remodel their chitin-containing cell walls. Although numerous chitinolytic enz...

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Autores principales:	Zhanliang Liu, Laurie M. Gay, Tina R. Tuveng, Jane W. Agger, Bjørge Westereng, Geir Mathiesen, Svein J. Horn, Gustav Vaaje-Kolstad, Daan M. F. van Aalten, Vincent G. H. Eijsink
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f472978cdfdc47b99927ec6827d307b8
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spelling	oai:doaj.org-article:f472978cdfdc47b99927ec6827d307b82021-12-02T15:05:23ZStructure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A410.1038/s41598-017-02043-12045-2322https://doaj.org/article/f472978cdfdc47b99927ec6827d307b82017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-02043-1https://doaj.org/toc/2045-2322Abstract Enzymatic conversion of chitin, a β-1,4 linked polymer of N-acetylglucosamine, is of major interest in areas varying from the biorefining of chitin-rich waste streams to understanding how medically relevant fungi remodel their chitin-containing cell walls. Although numerous chitinolytic enzymes have been studied in detail, relatively little is known about enzymes capable of deacetylating chitin. We describe the structural and functional characterization of a 237 residue deacetylase (AnCDA) from Aspergillus nidulans FGSC A4. AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and acetylxylan, but not on peptidoglycan. The K m and k cat of AnCDA for the first deacetylation of penta-N-acetyl-chitopentaose are 72 µM and 1.4 s−1, respectively. Combining mass spectrometry and analyses of acetate release, it was shown that AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3–6 in a non-processive manner. Deacetylation of the reducing end sugar was much slower than deacetylation of the other sugars in chito-oligomers. These enzymatic characteristics are discussed in the light of the crystal structure of AnCDA, providing insight into how the chitin deacetylase may interact with its substrates. Interestingly, AnCDA activity on crystalline chitin was enhanced by a lytic polysaccharide monooxygenase that increases substrate accessibility by oxidative cleavage of the chitin chains.Zhanliang LiuLaurie M. GayTina R. TuvengJane W. AggerBjørge WesterengGeir MathiesenSvein J. HornGustav Vaaje-KolstadDaan M. F. van AaltenVincent G. H. EijsinkNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Zhanliang Liu Laurie M. Gay Tina R. Tuveng Jane W. Agger Bjørge Westereng Geir Mathiesen Svein J. Horn Gustav Vaaje-Kolstad Daan M. F. van Aalten Vincent G. H. Eijsink Structure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A4
description	Abstract Enzymatic conversion of chitin, a β-1,4 linked polymer of N-acetylglucosamine, is of major interest in areas varying from the biorefining of chitin-rich waste streams to understanding how medically relevant fungi remodel their chitin-containing cell walls. Although numerous chitinolytic enzymes have been studied in detail, relatively little is known about enzymes capable of deacetylating chitin. We describe the structural and functional characterization of a 237 residue deacetylase (AnCDA) from Aspergillus nidulans FGSC A4. AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and acetylxylan, but not on peptidoglycan. The K m and k cat of AnCDA for the first deacetylation of penta-N-acetyl-chitopentaose are 72 µM and 1.4 s−1, respectively. Combining mass spectrometry and analyses of acetate release, it was shown that AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3–6 in a non-processive manner. Deacetylation of the reducing end sugar was much slower than deacetylation of the other sugars in chito-oligomers. These enzymatic characteristics are discussed in the light of the crystal structure of AnCDA, providing insight into how the chitin deacetylase may interact with its substrates. Interestingly, AnCDA activity on crystalline chitin was enhanced by a lytic polysaccharide monooxygenase that increases substrate accessibility by oxidative cleavage of the chitin chains.
format	article
author	Zhanliang Liu Laurie M. Gay Tina R. Tuveng Jane W. Agger Bjørge Westereng Geir Mathiesen Svein J. Horn Gustav Vaaje-Kolstad Daan M. F. van Aalten Vincent G. H. Eijsink
author_facet	Zhanliang Liu Laurie M. Gay Tina R. Tuveng Jane W. Agger Bjørge Westereng Geir Mathiesen Svein J. Horn Gustav Vaaje-Kolstad Daan M. F. van Aalten Vincent G. H. Eijsink
author_sort	Zhanliang Liu
title	Structure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A4
title_short	Structure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A4
title_full	Structure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A4
title_fullStr	Structure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A4
title_full_unstemmed	Structure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A4
title_sort	structure and function of a broad-specificity chitin deacetylase from aspergillus nidulans fgsc a4
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/f472978cdfdc47b99927ec6827d307b8
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Structure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A4

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