Identification in the mould Hypocrea jecorina of a gene encoding an NADP(+): d-xylose dehydrogenase

A gene coding for an NADP(+)-dependent d-xylose dehydrogenase was identified in the mould Hypocrea jecorina (Trichoderma reesei). It was cloned from cDNA, the active enzyme was expressed in yeast and a histidine-tagged enzyme was purified and characterized. The enzyme had highest activity with d-xyl...

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Autores principales: Berghäll, Suvi, Hilditch, Satu, Penttilä, Merja, Richard, Peter
Formato: Texto
Lenguaje:English
Publicado: Blackwell Publishing Ltd 2007
Materias:
Research Letter
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2228372/
https://www.ncbi.nlm.nih.gov/pubmed/18031347
http://dx.doi.org/10.1111/j.1574-6968.2007.00969.x
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author Berghäll, Suvi
Hilditch, Satu
Penttilä, Merja
Richard, Peter
author_facet Berghäll, Suvi
Hilditch, Satu
Penttilä, Merja
Richard, Peter
author_sort Berghäll, Suvi
collection PubMed
description A gene coding for an NADP(+)-dependent d-xylose dehydrogenase was identified in the mould Hypocrea jecorina (Trichoderma reesei). It was cloned from cDNA, the active enzyme was expressed in yeast and a histidine-tagged enzyme was purified and characterized. The enzyme had highest activity with d-xylose and significantly smaller activities with other aldose sugars. The enzyme is specific for NADP(+). The K(m) values for d-xylose and NADP(+) are 43 mM and 250 μM, respectively. The role of this enzyme in H. jecorina is unclear because in this organism d-xylose is predominantly catabolized through a path with xylitol and d-xylulose as intermediates and the mould is unable to grow on d-xylonic acid.
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spelling pubmed-22283722008-02-13 Identification in the mould Hypocrea jecorina of a gene encoding an NADP(+): d-xylose dehydrogenase Berghäll, Suvi Hilditch, Satu Penttilä, Merja Richard, Peter FEMS Microbiol Lett Research Letter A gene coding for an NADP(+)-dependent d-xylose dehydrogenase was identified in the mould Hypocrea jecorina (Trichoderma reesei). It was cloned from cDNA, the active enzyme was expressed in yeast and a histidine-tagged enzyme was purified and characterized. The enzyme had highest activity with d-xylose and significantly smaller activities with other aldose sugars. The enzyme is specific for NADP(+). The K(m) values for d-xylose and NADP(+) are 43 mM and 250 μM, respectively. The role of this enzyme in H. jecorina is unclear because in this organism d-xylose is predominantly catabolized through a path with xylitol and d-xylulose as intermediates and the mould is unable to grow on d-xylonic acid. Blackwell Publishing Ltd 2007-12 2007-11 /pmc/articles/PMC2228372/ /pubmed/18031347 http://dx.doi.org/10.1111/j.1574-6968.2007.00969.x Text en © 2007 Federation of European Microbiological Societies https://creativecommons.org/licenses/by/2.5/ OnlineOpen articles are made available in accordance with the terms of the Creative Commons Deed, Attribution 2.5 (further details available from http://www.creativecommons.org), which allows Open Access dissemination of the article, but does not permit commercial exploitation or the creation of derivative works.
spellingShingle Research Letter
Berghäll, Suvi
Hilditch, Satu
Penttilä, Merja
Richard, Peter
Identification in the mould Hypocrea jecorina of a gene encoding an NADP(+): d-xylose dehydrogenase
title Identification in the mould Hypocrea jecorina of a gene encoding an NADP(+): d-xylose dehydrogenase
title_full Identification in the mould Hypocrea jecorina of a gene encoding an NADP(+): d-xylose dehydrogenase
title_fullStr Identification in the mould Hypocrea jecorina of a gene encoding an NADP(+): d-xylose dehydrogenase
title_full_unstemmed Identification in the mould Hypocrea jecorina of a gene encoding an NADP(+): d-xylose dehydrogenase
title_short Identification in the mould Hypocrea jecorina of a gene encoding an NADP(+): d-xylose dehydrogenase
title_sort identification in the mould hypocrea jecorina of a gene encoding an nadp(+): d-xylose dehydrogenase
topic Research Letter
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2228372/
https://www.ncbi.nlm.nih.gov/pubmed/18031347
http://dx.doi.org/10.1111/j.1574-6968.2007.00969.x
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