Molecular cloning and 3D structure prediction of the first raw-starch-degrading glucoamylase without a separate starch-binding domain
Raw-starch-degrading glucoamylases have been known as multidomain enzymes consisting of a catalytic domain connected to a starch-binding domain (SBD) by an O-glycosylated linker region. A molecular genetics approach has been chosen to find structural differences between two related glucoamylases, ra...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 2003-03, Vol.411 (2), p.189-195 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Hostinová, Eva Solovicová, Adriana Dvorský, Radovan Gašperı́k, Juraj |
| description | Raw-starch-degrading glucoamylases have been known as multidomain enzymes consisting of a catalytic domain connected to a starch-binding domain (SBD) by an O-glycosylated linker region. A molecular genetics approach has been chosen to find structural differences between two related glucoamylases, raw-starch-degrading Glm and nondegrading Glu, from the yeasts
Saccharomycopsis fibuligera IFO 0111 and HUT 7212, respectively. We have found that Glm and Glu show a high primary (77%) and tertiary structure similarity. Glm, although possessing a good ability for raw starch degradation, did not show consensus amino acid residues to any SBD found in glucoamylases or other amylolytic enzymes. Raw starch binding and digestion by Glm must thus depend on the existence of a site(s) lying within the intact protein which lacks a separate SBD. The enzyme represents a structurally new type of raw-starch-degrading glucoamylase. |
| doi_str_mv | 10.1016/S0003-9861(03)00003-1 |
| format | Article |
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Saccharomycopsis fibuligera IFO 0111 and HUT 7212, respectively. We have found that Glm and Glu show a high primary (77%) and tertiary structure similarity. Glm, although possessing a good ability for raw starch degradation, did not show consensus amino acid residues to any SBD found in glucoamylases or other amylolytic enzymes. Raw starch binding and digestion by Glm must thus depend on the existence of a site(s) lying within the intact protein which lacks a separate SBD. The enzyme represents a structurally new type of raw-starch-degrading glucoamylase.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/S0003-9861(03)00003-1</identifier><identifier>PMID: 12623067</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Binding Sites ; Cloning, Molecular ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Glucan 1,4-alpha-Glucosidase - chemistry ; Glucan 1,4-alpha-Glucosidase - genetics ; Glucan 1,4-alpha-Glucosidase - metabolism ; Glucoamylase ; Imaging, Three-Dimensional ; Models, Molecular ; Molecular Sequence Data ; Primary structure ; Protein Conformation ; Raw starch ; Saccharomycopsis - enzymology ; Saccharomycopsis - genetics ; Saccharomycopsis fibuligera ; Sequence Homology, Amino Acid ; Starch - metabolism ; Starch-binding domain ; Structural Homology, Protein ; Tertiary structure model</subject><ispartof>Archives of biochemistry and biophysics, 2003-03, Vol.411 (2), p.189-195</ispartof><rights>2003 Elsevier Science (USA)</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c413t-aefa86ac2720483ef2944332853b1d04b5f91ef56b975e7d6d60f91b1a9e11973</citedby><cites>FETCH-LOGICAL-c413t-aefa86ac2720483ef2944332853b1d04b5f91ef56b975e7d6d60f91b1a9e11973</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0003986103000031$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12623067$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hostinová, Eva</creatorcontrib><creatorcontrib>Solovicová, Adriana</creatorcontrib><creatorcontrib>Dvorský, Radovan</creatorcontrib><creatorcontrib>Gašperı́k, Juraj</creatorcontrib><title>Molecular cloning and 3D structure prediction of the first raw-starch-degrading glucoamylase without a separate starch-binding domain</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Raw-starch-degrading glucoamylases have been known as multidomain enzymes consisting of a catalytic domain connected to a starch-binding domain (SBD) by an O-glycosylated linker region. A molecular genetics approach has been chosen to find structural differences between two related glucoamylases, raw-starch-degrading Glm and nondegrading Glu, from the yeasts
Saccharomycopsis fibuligera IFO 0111 and HUT 7212, respectively. We have found that Glm and Glu show a high primary (77%) and tertiary structure similarity. Glm, although possessing a good ability for raw starch degradation, did not show consensus amino acid residues to any SBD found in glucoamylases or other amylolytic enzymes. Raw starch binding and digestion by Glm must thus depend on the existence of a site(s) lying within the intact protein which lacks a separate SBD. The enzyme represents a structurally new type of raw-starch-degrading glucoamylase.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Cloning, Molecular</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Glucan 1,4-alpha-Glucosidase - chemistry</subject><subject>Glucan 1,4-alpha-Glucosidase - genetics</subject><subject>Glucan 1,4-alpha-Glucosidase - metabolism</subject><subject>Glucoamylase</subject><subject>Imaging, Three-Dimensional</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Primary structure</subject><subject>Protein Conformation</subject><subject>Raw starch</subject><subject>Saccharomycopsis - enzymology</subject><subject>Saccharomycopsis - genetics</subject><subject>Saccharomycopsis fibuligera</subject><subject>Sequence Homology, Amino Acid</subject><subject>Starch - metabolism</subject><subject>Starch-binding domain</subject><subject>Structural Homology, Protein</subject><subject>Tertiary structure model</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMuO1TAMhiMEYg4DjwDKCsGiYDdt2q7QaLhKg1gA68hN3HOC2uaQpIzmAXhvei6CJSvL1vfb8ifEU4RXCKhffwUAVXStxhegXsKxw3tig9DpAlRb3Rebv8iFeJTSDwDESpcPxQWWulSgm434_TmMbJeRorRjmP28lTQ7qd7KlONi8xJZ7iM7b7MPswyDzDuWg48py0i3RcoU7a5wvI3kDuntuNhA091IieWtz7uwZEky8Z4iZZbnQO_nI-7CRH5-LB4MNCZ-cq6X4vv7d9-uPxY3Xz58ur66KWyFKhfEA7WabNmUULWKh7KrKqXKtlY9Oqj6euiQh1r3XVNz47TTsE56pI4Ru0ZdiuenvfsYfi6cspl8sjyONHNYkmkUNF0DegXrE2hjSCnyYPbRTxTvDII5-DdH_-Yg16z16N_gmnt2PrD0E7t_qbPwFXhzAnh985fnaJL1PNvVcGSbjQv-Pyf-ACeKlwQ</recordid><startdate>20030315</startdate><enddate>20030315</enddate><creator>Hostinová, Eva</creator><creator>Solovicová, Adriana</creator><creator>Dvorský, Radovan</creator><creator>Gašperı́k, Juraj</creator><general>Elsevier Inc</general><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>7X8</scope></search><sort><creationdate>20030315</creationdate><title>Molecular cloning and 3D structure prediction of the first raw-starch-degrading glucoamylase without a separate starch-binding domain</title><author>Hostinová, Eva ; Solovicová, Adriana ; Dvorský, Radovan ; Gašperı́k, Juraj</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c413t-aefa86ac2720483ef2944332853b1d04b5f91ef56b975e7d6d60f91b1a9e11973</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Cloning, Molecular</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Glucan 1,4-alpha-Glucosidase - chemistry</topic><topic>Glucan 1,4-alpha-Glucosidase - genetics</topic><topic>Glucan 1,4-alpha-Glucosidase - metabolism</topic><topic>Glucoamylase</topic><topic>Imaging, Three-Dimensional</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Primary structure</topic><topic>Protein Conformation</topic><topic>Raw starch</topic><topic>Saccharomycopsis - enzymology</topic><topic>Saccharomycopsis - genetics</topic><topic>Saccharomycopsis fibuligera</topic><topic>Sequence Homology, Amino Acid</topic><topic>Starch - metabolism</topic><topic>Starch-binding domain</topic><topic>Structural Homology, Protein</topic><topic>Tertiary structure model</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hostinová, Eva</creatorcontrib><creatorcontrib>Solovicová, Adriana</creatorcontrib><creatorcontrib>Dvorský, Radovan</creatorcontrib><creatorcontrib>Gašperı́k, Juraj</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hostinová, Eva</au><au>Solovicová, Adriana</au><au>Dvorský, Radovan</au><au>Gašperı́k, Juraj</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular cloning and 3D structure prediction of the first raw-starch-degrading glucoamylase without a separate starch-binding domain</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>2003-03-15</date><risdate>2003</risdate><volume>411</volume><issue>2</issue><spage>189</spage><epage>195</epage><pages>189-195</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>Raw-starch-degrading glucoamylases have been known as multidomain enzymes consisting of a catalytic domain connected to a starch-binding domain (SBD) by an O-glycosylated linker region. A molecular genetics approach has been chosen to find structural differences between two related glucoamylases, raw-starch-degrading Glm and nondegrading Glu, from the yeasts
Saccharomycopsis fibuligera IFO 0111 and HUT 7212, respectively. We have found that Glm and Glu show a high primary (77%) and tertiary structure similarity. Glm, although possessing a good ability for raw starch degradation, did not show consensus amino acid residues to any SBD found in glucoamylases or other amylolytic enzymes. Raw starch binding and digestion by Glm must thus depend on the existence of a site(s) lying within the intact protein which lacks a separate SBD. The enzyme represents a structurally new type of raw-starch-degrading glucoamylase.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12623067</pmid><doi>10.1016/S0003-9861(03)00003-1</doi><tpages>7</tpages></addata></record> |
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| subjects | Amino Acid Sequence Binding Sites Cloning, Molecular Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism Glucan 1,4-alpha-Glucosidase - chemistry Glucan 1,4-alpha-Glucosidase - genetics Glucan 1,4-alpha-Glucosidase - metabolism Glucoamylase Imaging, Three-Dimensional Models, Molecular Molecular Sequence Data Primary structure Protein Conformation Raw starch Saccharomycopsis - enzymology Saccharomycopsis - genetics Saccharomycopsis fibuligera Sequence Homology, Amino Acid Starch - metabolism Starch-binding domain Structural Homology, Protein Tertiary structure model |
| title | Molecular cloning and 3D structure prediction of the first raw-starch-degrading glucoamylase without a separate starch-binding domain |
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