Loading…

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-xylos...

Full description

Saved in:
Bibliographic Details
Published in:FEMS microbiology letters 2007-12, Vol.277 (2), p.249-253
Main Authors: Berghäll, Suvi, Hilditch, Satu, Penttilä, Merja, Richard, Peter
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c5479-1c48326a2241f74c016a8dc03e4fbb792ef65b6a7f41e53e2bacb84a3a8209373
cites cdi_FETCH-LOGICAL-c5479-1c48326a2241f74c016a8dc03e4fbb792ef65b6a7f41e53e2bacb84a3a8209373
container_end_page 253
container_issue 2
container_start_page 249
container_title FEMS microbiology letters
container_volume 277
creator Berghäll, Suvi
Hilditch, Satu
Penttilä, Merja
Richard, Peter
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 Km 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.
doi_str_mv 10.1111/j.1574-6968.2007.00969.x
format article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2228372</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><oup_id>10.1111/j.1574-6968.2007.00969.x</oup_id><sourcerecordid>68543105</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5479-1c48326a2241f74c016a8dc03e4fbb792ef65b6a7f41e53e2bacb84a3a8209373</originalsourceid><addsrcrecordid>eNqNkd-KEzEUxgdR3Lr6ChoQvZt68meSjCzCsrruQv0Dutchk8m0KdOkJh3tXPpaPo5PYmrLroqCuTmB8_sO38dXFAjDFOf3bDnFlWAlr7mcEgAxBah5Pd3eKibXi9vFBKiQJYZaHBX3UloCACPA7xZHWALFlIlJYS5b6zeuc0ZvXPDIebRZWLQKQ9-ii3EdTLQaLa0J0XmNQoc0mltvkfUmtM7Pkfbo7enL99-_fnuO2nI79iFZ1NrF2MaQSZ3s_eJOp_tkHxzmcXF1_urj2UU5e_f68ux0VpqKibrEhklKuCaE4U4wA5hr2RqglnVNI2piO141XIuOYVtRSxptGsk01ZJATQU9Ll7s766HZmVbk4NF3at1dCsdRxW0U79vvFuoefisCCGSCpIPPD0ciOHTYNNGrVwytu-1t2FIisuKUQxVBh__AS7DEH0OpwgFXlFS4R0l95SJIaVou2srGNSuR7VUu7rUri6161H97FFts_Thr1FuhIfiMvDkAOhkdN9F7Y1LN1wthQDOMney57643o7_bUCdv5nlT5bTvTwM63-Iy7-5f7RXdTooPY_Z2NUHApgCSFJL4PQHDfTSKg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2306532515</pqid></control><display><type>article</type><title>Identification in the mould Hypocrea jecorina of a gene encoding an NADP⁺: d-xylose dehydrogenase</title><source>Oxford Journals Online</source><creator>Berghäll, Suvi ; Hilditch, Satu ; Penttilä, Merja ; Richard, Peter</creator><creatorcontrib>Berghäll, Suvi ; Hilditch, Satu ; Penttilä, Merja ; Richard, Peter</creatorcontrib><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 Km 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.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2007.00969.x</identifier><identifier>PMID: 18031347</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Oxford, UK : Blackwell Publishing Ltd</publisher><subject>Aldehyde Reductase - genetics ; Aldehyde Reductase - metabolism ; Biological and medical sciences ; d-xylose dehydrogenase ; d-xylose metabolism ; Dehydrogenase ; Dehydrogenases ; DNA, Complementary - isolation &amp; purification ; EC 1.1.1.175 ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Fungi ; Gene Expression ; Growth, nutrition, metabolism, transports, enzymes. Molecular biology ; Histidine ; Hypocrea - enzymology ; Hypocrea - genetics ; Hypocrea jecorina ; Intermediates ; Kinetics ; Microbiology ; Molecular Sequence Data ; Mycology ; NADP ; NADP-linked d-xylose dehydrogenase ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation &amp; purification ; Recombinant Proteins - metabolism ; Research Letter ; Saccharomyces cerevisiae - genetics ; Substrate Specificity ; Sugar ; Trichoderma reesei ; Xylitol ; Xylose ; Xylose - metabolism ; Xylulose ; Yeast ; Yeasts</subject><ispartof>FEMS microbiology letters, 2007-12, Vol.277 (2), p.249-253</ispartof><rights>2007 Federation of European Microbiological Societies 2007</rights><rights>2008 INIST-CNRS</rights><rights>2007 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5479-1c48326a2241f74c016a8dc03e4fbb792ef65b6a7f41e53e2bacb84a3a8209373</citedby><cites>FETCH-LOGICAL-c5479-1c48326a2241f74c016a8dc03e4fbb792ef65b6a7f41e53e2bacb84a3a8209373</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=19877064$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18031347$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Berghäll, Suvi</creatorcontrib><creatorcontrib>Hilditch, Satu</creatorcontrib><creatorcontrib>Penttilä, Merja</creatorcontrib><creatorcontrib>Richard, Peter</creatorcontrib><title>Identification in the mould Hypocrea jecorina of a gene encoding an NADP⁺: d-xylose dehydrogenase</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><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 Km 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.</description><subject>Aldehyde Reductase - genetics</subject><subject>Aldehyde Reductase - metabolism</subject><subject>Biological and medical sciences</subject><subject>d-xylose dehydrogenase</subject><subject>d-xylose metabolism</subject><subject>Dehydrogenase</subject><subject>Dehydrogenases</subject><subject>DNA, Complementary - isolation &amp; purification</subject><subject>EC 1.1.1.175</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Fungi</subject><subject>Gene Expression</subject><subject>Growth, nutrition, metabolism, transports, enzymes. Molecular biology</subject><subject>Histidine</subject><subject>Hypocrea - enzymology</subject><subject>Hypocrea - genetics</subject><subject>Hypocrea jecorina</subject><subject>Intermediates</subject><subject>Kinetics</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Mycology</subject><subject>NADP</subject><subject>NADP-linked d-xylose dehydrogenase</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation &amp; purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Research Letter</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Substrate Specificity</subject><subject>Sugar</subject><subject>Trichoderma reesei</subject><subject>Xylitol</subject><subject>Xylose</subject><subject>Xylose - metabolism</subject><subject>Xylulose</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><recordid>eNqNkd-KEzEUxgdR3Lr6ChoQvZt68meSjCzCsrruQv0Dutchk8m0KdOkJh3tXPpaPo5PYmrLroqCuTmB8_sO38dXFAjDFOf3bDnFlWAlr7mcEgAxBah5Pd3eKibXi9vFBKiQJYZaHBX3UloCACPA7xZHWALFlIlJYS5b6zeuc0ZvXPDIebRZWLQKQ9-ii3EdTLQaLa0J0XmNQoc0mltvkfUmtM7Pkfbo7enL99-_fnuO2nI79iFZ1NrF2MaQSZ3s_eJOp_tkHxzmcXF1_urj2UU5e_f68ux0VpqKibrEhklKuCaE4U4wA5hr2RqglnVNI2piO141XIuOYVtRSxptGsk01ZJATQU9Ll7s766HZmVbk4NF3at1dCsdRxW0U79vvFuoefisCCGSCpIPPD0ciOHTYNNGrVwytu-1t2FIisuKUQxVBh__AS7DEH0OpwgFXlFS4R0l95SJIaVou2srGNSuR7VUu7rUri6161H97FFts_Thr1FuhIfiMvDkAOhkdN9F7Y1LN1wthQDOMney57643o7_bUCdv5nlT5bTvTwM63-Iy7-5f7RXdTooPY_Z2NUHApgCSFJL4PQHDfTSKg</recordid><startdate>200712</startdate><enddate>200712</enddate><creator>Berghäll, Suvi</creator><creator>Hilditch, Satu</creator><creator>Penttilä, Merja</creator><creator>Richard, Peter</creator><general>Oxford, UK : Blackwell Publishing Ltd</general><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</general><scope>FBQ</scope><scope>24P</scope><scope>WIN</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200712</creationdate><title>Identification in the mould Hypocrea jecorina of a gene encoding an NADP⁺: d-xylose dehydrogenase</title><author>Berghäll, Suvi ; Hilditch, Satu ; Penttilä, Merja ; Richard, Peter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5479-1c48326a2241f74c016a8dc03e4fbb792ef65b6a7f41e53e2bacb84a3a8209373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Aldehyde Reductase - genetics</topic><topic>Aldehyde Reductase - metabolism</topic><topic>Biological and medical sciences</topic><topic>d-xylose dehydrogenase</topic><topic>d-xylose metabolism</topic><topic>Dehydrogenase</topic><topic>Dehydrogenases</topic><topic>DNA, Complementary - isolation &amp; purification</topic><topic>EC 1.1.1.175</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Fungi</topic><topic>Gene Expression</topic><topic>Growth, nutrition, metabolism, transports, enzymes. Molecular biology</topic><topic>Histidine</topic><topic>Hypocrea - enzymology</topic><topic>Hypocrea - genetics</topic><topic>Hypocrea jecorina</topic><topic>Intermediates</topic><topic>Kinetics</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Mycology</topic><topic>NADP</topic><topic>NADP-linked d-xylose dehydrogenase</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - isolation &amp; purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Research Letter</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Substrate Specificity</topic><topic>Sugar</topic><topic>Trichoderma reesei</topic><topic>Xylitol</topic><topic>Xylose</topic><topic>Xylose - metabolism</topic><topic>Xylulose</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Berghäll, Suvi</creatorcontrib><creatorcontrib>Hilditch, Satu</creatorcontrib><creatorcontrib>Penttilä, Merja</creatorcontrib><creatorcontrib>Richard, Peter</creatorcontrib><collection>AGRIS</collection><collection>Wiley Online Library Open Access</collection><collection>Wiley Free Archive</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Databases</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Berghäll, Suvi</au><au>Hilditch, Satu</au><au>Penttilä, Merja</au><au>Richard, Peter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification in the mould Hypocrea jecorina of a gene encoding an NADP⁺: d-xylose dehydrogenase</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2007-12</date><risdate>2007</risdate><volume>277</volume><issue>2</issue><spage>249</spage><epage>253</epage><pages>249-253</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>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 Km 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.</abstract><cop>Oxford, UK</cop><pub>Oxford, UK : Blackwell Publishing Ltd</pub><pmid>18031347</pmid><doi>10.1111/j.1574-6968.2007.00969.x</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0378-1097
ispartof FEMS microbiology letters, 2007-12, Vol.277 (2), p.249-253
issn 0378-1097
1574-6968
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2228372
source Oxford Journals Online
subjects Aldehyde Reductase - genetics
Aldehyde Reductase - metabolism
Biological and medical sciences
d-xylose dehydrogenase
d-xylose metabolism
Dehydrogenase
Dehydrogenases
DNA, Complementary - isolation & purification
EC 1.1.1.175
Enzymes
Fundamental and applied biological sciences. Psychology
Fungal Proteins - genetics
Fungal Proteins - metabolism
Fungi
Gene Expression
Growth, nutrition, metabolism, transports, enzymes. Molecular biology
Histidine
Hypocrea - enzymology
Hypocrea - genetics
Hypocrea jecorina
Intermediates
Kinetics
Microbiology
Molecular Sequence Data
Mycology
NADP
NADP-linked d-xylose dehydrogenase
Recombinant Proteins - genetics
Recombinant Proteins - isolation & purification
Recombinant Proteins - metabolism
Research Letter
Saccharomyces cerevisiae - genetics
Substrate Specificity
Sugar
Trichoderma reesei
Xylitol
Xylose
Xylose - metabolism
Xylulose
Yeast
Yeasts
title Identification in the mould Hypocrea jecorina of a gene encoding an NADP⁺: d-xylose dehydrogenase
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-06T21%3A19%3A55IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Identification%20in%20the%20mould%20Hypocrea%20jecorina%20of%20a%20gene%20encoding%20an%20NADP%E2%81%BA:%20d-xylose%20dehydrogenase&rft.jtitle=FEMS%20microbiology%20letters&rft.au=Bergh%C3%A4ll,%20Suvi&rft.date=2007-12&rft.volume=277&rft.issue=2&rft.spage=249&rft.epage=253&rft.pages=249-253&rft.issn=0378-1097&rft.eissn=1574-6968&rft.coden=FMLED7&rft_id=info:doi/10.1111/j.1574-6968.2007.00969.x&rft_dat=%3Cproquest_pubme%3E68543105%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c5479-1c48326a2241f74c016a8dc03e4fbb792ef65b6a7f41e53e2bacb84a3a8209373%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2306532515&rft_id=info:pmid/18031347&rft_oup_id=10.1111/j.1574-6968.2007.00969.x&rfr_iscdi=true