Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe
Homoisocitrate dehydrogenase (HICDH) catalyzes the conversion of homoisocitrate to 2-oxoadipate, the third enzymatic step in the α-aminoadipate pathway by which lysine is synthesized in fungi and certain archaebacteria. This enzyme represents a potential target for anti-fungal drug design. Here, we...
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| Veröffentlicht in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2012-02, Vol.80 (2), p.661-666 |
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| creator | Bulfer, Stacie L. Hendershot, Jenna M. Trievel, Raymond C. |
| description | Homoisocitrate dehydrogenase (HICDH) catalyzes the conversion of homoisocitrate to 2-oxoadipate, the third enzymatic step in the α-aminoadipate pathway by which lysine is synthesized in fungi and certain archaebacteria. This enzyme represents a potential target for anti-fungal drug design. Here, we describe the first crystal structures of a fungal HICDH, including structures of an apoenzyme and a binary complex with a glycine tri-peptide. The structures illustrate the homology of HICDH with other β-hydroxyacid oxidative decarboxylases and reveal key differences with the active site of Thermus thermophilus HICDH that provide insights into the differences in substrate specificity of these enzymes. |
| doi_str_mv | 10.1002/prot.23231 |
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(ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><description>Homoisocitrate dehydrogenase (HICDH) catalyzes the conversion of homoisocitrate to 2-oxoadipate, the third enzymatic step in the α-aminoadipate pathway by which lysine is synthesized in fungi and certain archaebacteria. This enzyme represents a potential target for anti-fungal drug design. Here, we describe the first crystal structures of a fungal HICDH, including structures of an apoenzyme and a binary complex with a glycine tri-peptide. 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(ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe</title><title>Proteins, structure, function, and bioinformatics</title><addtitle>Proteins</addtitle><description>Homoisocitrate dehydrogenase (HICDH) catalyzes the conversion of homoisocitrate to 2-oxoadipate, the third enzymatic step in the α-aminoadipate pathway by which lysine is synthesized in fungi and certain archaebacteria. This enzyme represents a potential target for anti-fungal drug design. Here, we describe the first crystal structures of a fungal HICDH, including structures of an apoenzyme and a binary complex with a glycine tri-peptide. The structures illustrate the homology of HICDH with other β-hydroxyacid oxidative decarboxylases and reveal key differences with the active site of Thermus thermophilus HICDH that provide insights into the differences in substrate specificity of these enzymes.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>ADDITIVES</subject><subject>Alcohol Oxidoreductases - chemistry</subject><subject>Alcohol Oxidoreductases - metabolism</subject><subject>amino acid metabolism</subject><subject>AMINO ACIDS</subject><subject>ASPERGILLUS</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BIOSYNTHESIS</subject><subject>CANDIDA</subject><subject>Catalytic Domain</subject><subject>CITRIC ACID</subject><subject>CRYSTAL STRUCTURE</subject><subject>CRYSTALLOGRAPHY</subject><subject>Crystallography, X-Ray</subject><subject>DECARBOXYLASES</subject><subject>DECARBOXYLATION</subject><subject>ENZYMES</subject><subject>EUGLENA</subject><subject>FUNGI</subject><subject>LEUCINE</subject><subject>LYSINE</subject><subject>lysine biosynthesis</subject><subject>METABOLISM</subject><subject>Models, Molecular</subject><subject>NAD</subject><subject>OXIDOREDUCTASES</subject><subject>Protein Conformation</subject><subject>Schizosaccharomyces pombe Proteins - chemistry</subject><subject>Schizosaccharomyces pombe Proteins - metabolism</subject><subject>Structural Homology, Protein</subject><subject>SUBSTRATES</subject><subject>TARTRATES</subject><subject>X-ray crystallography</subject><subject>β-hydroxyacid oxidative decarboxylase</subject><issn>0887-3585</issn><issn>1097-0134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU9v1DAQxS0EokvhwgdAEVwQUor_xYkvSGgFBWm1regiJC6W40walyRebAcInx6XtCvgwMka-Tdv5s1D6DHBJwRj-nLvXTyhjDJyB60IlmWOCeN30QpXVZmzoiqO0IMQrjDGQjJxHx1RSnBRcrZC52s_h6j7LEQ_mTh5yFybdW5wNjhjo9cRsga6ufHuEkYdIGu9G7IL09mfLmhjOp3q2UDI9m6o4SG61-o-wKOb9xh9fPtmt36Xb85O369fb3JTlJLkUFW8aQvTkEozIiteNppiKuqaVBw0ZVDIGniFoWBag2kbiVnFBG8LKQjU7Bi9WnT3Uz1AY2BMu_Zq7-2g_aycturvn9F26tJ9U5wxWhKSBJ4uAi5Eq0LyCqYzbhzBREUw41LQBD2_meLd1wlCVIMNBvpej-CmoIigKQHCRJnQZ_-gV27yY7qBIlQITgUmMlEvFsp4F4KH9rAxweo6TXWdpvqdZoKf_OnxgN7GlwCyAN9tD_N_pNT5h7PdrWi-9NgQ4cehR_svKrkoC_Vpe6o2ku22u88Xast-AbgUuz0</recordid><startdate>201202</startdate><enddate>201202</enddate><creator>Bulfer, Stacie L.</creator><creator>Hendershot, Jenna M.</creator><creator>Trievel, Raymond C.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</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>7QL</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>201202</creationdate><title>Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe</title><author>Bulfer, Stacie L. ; Hendershot, Jenna M. ; Trievel, Raymond C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5791-e884df5cd18a319847da2026bb184ea23e59be480e53aaecfd9038364f5961eb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>ADDITIVES</topic><topic>Alcohol Oxidoreductases - chemistry</topic><topic>Alcohol Oxidoreductases - metabolism</topic><topic>amino acid metabolism</topic><topic>AMINO ACIDS</topic><topic>ASPERGILLUS</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BIOSYNTHESIS</topic><topic>CANDIDA</topic><topic>Catalytic Domain</topic><topic>CITRIC ACID</topic><topic>CRYSTAL STRUCTURE</topic><topic>CRYSTALLOGRAPHY</topic><topic>Crystallography, X-Ray</topic><topic>DECARBOXYLASES</topic><topic>DECARBOXYLATION</topic><topic>ENZYMES</topic><topic>EUGLENA</topic><topic>FUNGI</topic><topic>LEUCINE</topic><topic>LYSINE</topic><topic>lysine biosynthesis</topic><topic>METABOLISM</topic><topic>Models, Molecular</topic><topic>NAD</topic><topic>OXIDOREDUCTASES</topic><topic>Protein Conformation</topic><topic>Schizosaccharomyces pombe Proteins - chemistry</topic><topic>Schizosaccharomyces pombe Proteins - metabolism</topic><topic>Structural Homology, Protein</topic><topic>SUBSTRATES</topic><topic>TARTRATES</topic><topic>X-ray crystallography</topic><topic>β-hydroxyacid oxidative decarboxylase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bulfer, Stacie L.</creatorcontrib><creatorcontrib>Hendershot, Jenna M.</creatorcontrib><creatorcontrib>Trievel, Raymond C.</creatorcontrib><creatorcontrib>Argonne National Lab. 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(ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe</atitle><jtitle>Proteins, structure, function, and bioinformatics</jtitle><addtitle>Proteins</addtitle><date>2012-02</date><risdate>2012</risdate><volume>80</volume><issue>2</issue><spage>661</spage><epage>666</epage><pages>661-666</pages><issn>0887-3585</issn><eissn>1097-0134</eissn><abstract>Homoisocitrate dehydrogenase (HICDH) catalyzes the conversion of homoisocitrate to 2-oxoadipate, the third enzymatic step in the α-aminoadipate pathway by which lysine is synthesized in fungi and certain archaebacteria. This enzyme represents a potential target for anti-fungal drug design. Here, we describe the first crystal structures of a fungal HICDH, including structures of an apoenzyme and a binary complex with a glycine tri-peptide. 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| ispartof | Proteins, structure, function, and bioinformatics, 2012-02, Vol.80 (2), p.661-666 |
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| subjects | 60 APPLIED LIFE SCIENCES ADDITIVES Alcohol Oxidoreductases - chemistry Alcohol Oxidoreductases - metabolism amino acid metabolism AMINO ACIDS ASPERGILLUS BASIC BIOLOGICAL SCIENCES BIOSYNTHESIS CANDIDA Catalytic Domain CITRIC ACID CRYSTAL STRUCTURE CRYSTALLOGRAPHY Crystallography, X-Ray DECARBOXYLASES DECARBOXYLATION ENZYMES EUGLENA FUNGI LEUCINE LYSINE lysine biosynthesis METABOLISM Models, Molecular NAD OXIDOREDUCTASES Protein Conformation Schizosaccharomyces pombe Proteins - chemistry Schizosaccharomyces pombe Proteins - metabolism Structural Homology, Protein SUBSTRATES TARTRATES X-ray crystallography β-hydroxyacid oxidative decarboxylase |
| title | Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe |
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