Cloning and Expression of a Fungal l-Arabinitol 4-Dehydrogenase Gene
l-Arabinitol 4-dehydrogenase (EC 1.1.1.12) was purified from the filamentous fungusTrichoderma reesei (Hypocrea jecorina). It is an enzyme in the l-arabinose catabolic pathway of fungi catalyzing the reaction from l-arabinitol tol-xylulose. The amino acid sequence of peptide fragments was determined...
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| Veröffentlicht in: | The Journal of biological chemistry 2001-11, Vol.276 (44), p.40631-40637 |
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| creator | Richard, Peter Londesborough, John Putkonen, Mikko Kalkkinen, Nisse Penttilä, Merja |
| description | l-Arabinitol 4-dehydrogenase (EC 1.1.1.12) was purified from the filamentous fungusTrichoderma reesei (Hypocrea jecorina). It is an enzyme in the l-arabinose catabolic pathway of fungi catalyzing the reaction from l-arabinitol tol-xylulose. The amino acid sequence of peptide fragments was determined and used to identify the corresponding gene. We named the gene lad1. It is not constitutively expressed. In a Northern analysis we found it only after growth onl-arabinose. The gene was cloned and overexpressed inSaccharomyces cerevisiae, and the enzyme activity was confirmed in a cell extract. The enzyme consists of 377 amino acids and has a calculated molecular mass of 39,822 Da. It belongs to the family of zinc-binding dehydrogenases and has some amino acid sequence similarity to sorbitol dehydrogenases. It shows activity towardl-arabinitol, adonitol (ribitol), and xylitol withKm values of about 40 mm towardl-arabinitol and adonitol and about 180 mmtoward xylitol. No activity was observed with d-sorbitol,d-arabinitol, and d-mannitol. NAD is the required cofactor with a Km of 180 µm. No activity was observed with NADP. |
| doi_str_mv | 10.1074/jbc.M104022200 |
| format | Article |
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It is an enzyme in the l-arabinose catabolic pathway of fungi catalyzing the reaction from l-arabinitol tol-xylulose. The amino acid sequence of peptide fragments was determined and used to identify the corresponding gene. We named the gene lad1. It is not constitutively expressed. In a Northern analysis we found it only after growth onl-arabinose. The gene was cloned and overexpressed inSaccharomyces cerevisiae, and the enzyme activity was confirmed in a cell extract. The enzyme consists of 377 amino acids and has a calculated molecular mass of 39,822 Da. It belongs to the family of zinc-binding dehydrogenases and has some amino acid sequence similarity to sorbitol dehydrogenases. It shows activity towardl-arabinitol, adonitol (ribitol), and xylitol withKm values of about 40 mm towardl-arabinitol and adonitol and about 180 mmtoward xylitol. No activity was observed with d-sorbitol,d-arabinitol, and d-mannitol. NAD is the required cofactor with a Km of 180 µm. No activity was observed with NADP.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M104022200</identifier><identifier>PMID: 11514550</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; DNA, Complementary ; Electrophoresis, Polyacrylamide Gel ; Kinetics ; L-Arabinitol ; L-Arabinitol 4-dehydrogenase ; L-Xylulose ; lad1 gene ; Molecular Sequence Data ; NAD ; Peptide Mapping ; Saccharomyces cerevisiae ; Sequence Homology, Amino Acid ; Sugar Alcohol Dehydrogenases - chemistry ; Sugar Alcohol Dehydrogenases - genetics ; Sugar Alcohol Dehydrogenases - isolation & purification ; Sugar Alcohol Dehydrogenases - metabolism ; Trichoderma - enzymology ; Trichoderma - genetics ; Trichoderma reesei</subject><ispartof>The Journal of biological chemistry, 2001-11, Vol.276 (44), p.40631-40637</ispartof><rights>2001 © 2001 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c551t-7c958737e0f0e126363a77a9bd71d50162c88b4d157a3e9aa2c3cc7546f384463</citedby><cites>FETCH-LOGICAL-c551t-7c958737e0f0e126363a77a9bd71d50162c88b4d157a3e9aa2c3cc7546f384463</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11514550$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Richard, Peter</creatorcontrib><creatorcontrib>Londesborough, John</creatorcontrib><creatorcontrib>Putkonen, Mikko</creatorcontrib><creatorcontrib>Kalkkinen, Nisse</creatorcontrib><creatorcontrib>Penttilä, Merja</creatorcontrib><title>Cloning and Expression of a Fungal l-Arabinitol 4-Dehydrogenase Gene</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>l-Arabinitol 4-dehydrogenase (EC 1.1.1.12) was purified from the filamentous fungusTrichoderma reesei (Hypocrea jecorina). It is an enzyme in the l-arabinose catabolic pathway of fungi catalyzing the reaction from l-arabinitol tol-xylulose. The amino acid sequence of peptide fragments was determined and used to identify the corresponding gene. We named the gene lad1. It is not constitutively expressed. In a Northern analysis we found it only after growth onl-arabinose. The gene was cloned and overexpressed inSaccharomyces cerevisiae, and the enzyme activity was confirmed in a cell extract. The enzyme consists of 377 amino acids and has a calculated molecular mass of 39,822 Da. It belongs to the family of zinc-binding dehydrogenases and has some amino acid sequence similarity to sorbitol dehydrogenases. It shows activity towardl-arabinitol, adonitol (ribitol), and xylitol withKm values of about 40 mm towardl-arabinitol and adonitol and about 180 mmtoward xylitol. No activity was observed with d-sorbitol,d-arabinitol, and d-mannitol. NAD is the required cofactor with a Km of 180 µm. No activity was observed with NADP.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Kinetics</subject><subject>L-Arabinitol</subject><subject>L-Arabinitol 4-dehydrogenase</subject><subject>L-Xylulose</subject><subject>lad1 gene</subject><subject>Molecular Sequence Data</subject><subject>NAD</subject><subject>Peptide Mapping</subject><subject>Saccharomyces cerevisiae</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sugar Alcohol Dehydrogenases - chemistry</subject><subject>Sugar Alcohol Dehydrogenases - genetics</subject><subject>Sugar Alcohol Dehydrogenases - isolation & purification</subject><subject>Sugar Alcohol Dehydrogenases - metabolism</subject><subject>Trichoderma - enzymology</subject><subject>Trichoderma - genetics</subject><subject>Trichoderma reesei</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0Ltv2zAQwGGiaNE4SdeOhYaim9w7PqUxcJ5Aii4tkI2gqJPNQCZd0s7jv68CG8gUhMst3x2IH2NfEeYIRv687_z8F4IEzjnABzZDaEQtFN59ZDMAjnXLVXPEjku5h-nJFj-zI0SFUimYsfPFmGKIy8rFvrp42mQqJaRYpaFy1eUuLt1YjfVZdl2IYZvGStbntHruc1pSdIWqK4p0yj4Nbiz05TBP2N_Liz-L6_r299XN4uy29krhtja-VY0RhmAAQq6FFs4Y13a9wV4Bau6bppM9KuMEtc5xL7w3SupBNFJqccJ-7O9ucvq3o7K161A8jaOLlHbFGs6F1sDfhdgglwhqgvM99DmVkmmwmxzWLj9bBPsS2E6B7WvgaeHb4fKuW1P_yg9FJ_B9D1ZhuXoMmWwXkl_R2nKjrZRWghY4sWbPaOr1ECjb4gNFT_204re2T-GtL_wHpvGSRg</recordid><startdate>20011102</startdate><enddate>20011102</enddate><creator>Richard, Peter</creator><creator>Londesborough, John</creator><creator>Putkonen, Mikko</creator><creator>Kalkkinen, Nisse</creator><creator>Penttilä, Merja</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20011102</creationdate><title>Cloning and Expression of a Fungal l-Arabinitol 4-Dehydrogenase Gene</title><author>Richard, Peter ; Londesborough, John ; Putkonen, Mikko ; Kalkkinen, Nisse ; Penttilä, Merja</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c551t-7c958737e0f0e126363a77a9bd71d50162c88b4d157a3e9aa2c3cc7546f384463</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Kinetics</topic><topic>L-Arabinitol</topic><topic>L-Arabinitol 4-dehydrogenase</topic><topic>L-Xylulose</topic><topic>lad1 gene</topic><topic>Molecular Sequence Data</topic><topic>NAD</topic><topic>Peptide Mapping</topic><topic>Saccharomyces cerevisiae</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sugar Alcohol Dehydrogenases - chemistry</topic><topic>Sugar Alcohol Dehydrogenases - genetics</topic><topic>Sugar Alcohol Dehydrogenases - isolation & purification</topic><topic>Sugar Alcohol Dehydrogenases - metabolism</topic><topic>Trichoderma - enzymology</topic><topic>Trichoderma - genetics</topic><topic>Trichoderma reesei</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Richard, Peter</creatorcontrib><creatorcontrib>Londesborough, John</creatorcontrib><creatorcontrib>Putkonen, Mikko</creatorcontrib><creatorcontrib>Kalkkinen, Nisse</creatorcontrib><creatorcontrib>Penttilä, Merja</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Richard, Peter</au><au>Londesborough, John</au><au>Putkonen, Mikko</au><au>Kalkkinen, Nisse</au><au>Penttilä, Merja</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and Expression of a Fungal l-Arabinitol 4-Dehydrogenase Gene</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2001-11-02</date><risdate>2001</risdate><volume>276</volume><issue>44</issue><spage>40631</spage><epage>40637</epage><pages>40631-40637</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>l-Arabinitol 4-dehydrogenase (EC 1.1.1.12) was purified from the filamentous fungusTrichoderma reesei (Hypocrea jecorina). It is an enzyme in the l-arabinose catabolic pathway of fungi catalyzing the reaction from l-arabinitol tol-xylulose. The amino acid sequence of peptide fragments was determined and used to identify the corresponding gene. We named the gene lad1. It is not constitutively expressed. In a Northern analysis we found it only after growth onl-arabinose. The gene was cloned and overexpressed inSaccharomyces cerevisiae, and the enzyme activity was confirmed in a cell extract. The enzyme consists of 377 amino acids and has a calculated molecular mass of 39,822 Da. It belongs to the family of zinc-binding dehydrogenases and has some amino acid sequence similarity to sorbitol dehydrogenases. It shows activity towardl-arabinitol, adonitol (ribitol), and xylitol withKm values of about 40 mm towardl-arabinitol and adonitol and about 180 mmtoward xylitol. No activity was observed with d-sorbitol,d-arabinitol, and d-mannitol. NAD is the required cofactor with a Km of 180 µm. No activity was observed with NADP.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11514550</pmid><doi>10.1074/jbc.M104022200</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Base Sequence Cloning, Molecular DNA, Complementary Electrophoresis, Polyacrylamide Gel Kinetics L-Arabinitol L-Arabinitol 4-dehydrogenase L-Xylulose lad1 gene Molecular Sequence Data NAD Peptide Mapping Saccharomyces cerevisiae Sequence Homology, Amino Acid Sugar Alcohol Dehydrogenases - chemistry Sugar Alcohol Dehydrogenases - genetics Sugar Alcohol Dehydrogenases - isolation & purification Sugar Alcohol Dehydrogenases - metabolism Trichoderma - enzymology Trichoderma - genetics Trichoderma reesei |
| title | Cloning and Expression of a Fungal l-Arabinitol 4-Dehydrogenase Gene |
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