Evidence for glycogenin autoglucosylation cessation by inaccessibility of the acquired maltosaccharide
Glycogenin initiates the biosynthesis of proteoglycogen, the mammalian glycogenin-bound glycogen, by intramolecular autoglucosylation. The incubation of glycogenin with UDP-glucose results in formation of a tyrosine-bound maltosaccharide, reaching maximum polymerization degree of 13 glucose units at...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2008-10, Vol.374 (4), p.704-708 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Romero, Jorge M. Issoglio, Federico M. Carrizo, María E. Curtino, Juan A. |
| description | Glycogenin initiates the biosynthesis of proteoglycogen, the mammalian glycogenin-bound glycogen, by intramolecular autoglucosylation. The incubation of glycogenin with UDP-glucose results in formation of a tyrosine-bound maltosaccharide, reaching maximum polymerization degree of 13 glucose units at cessation of the reaction. No exhaustion of the substrate donor occurred at the autoglucosylation end and the full autoglucosylated enzyme continued catalytically active for transglucosylation of the alternative substrate dodecyl-maltose. Even the autoglucosylation cessation once glycogenin acquired a mature maltosaccharide moiety, proteoglycogen and glycogenin species ranging rM 47–200
kDa, derived from proteoglycogen, showed to be autoglucosylable. The results describe for the first time the ability of polysaccharide-bound glycogenin for intramolecular autoglucosylation, providing evidence for cessation of the glucose polymerization initiated into the tyrosine residue, by inaccessibility of the acquired maltosaccharide moiety to further autoglucosylation. |
| doi_str_mv | 10.1016/j.bbrc.2008.07.114 |
| format | Article |
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kDa, derived from proteoglycogen, showed to be autoglucosylable. The results describe for the first time the ability of polysaccharide-bound glycogenin for intramolecular autoglucosylation, providing evidence for cessation of the glucose polymerization initiated into the tyrosine residue, by inaccessibility of the acquired maltosaccharide moiety to further autoglucosylation.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2008.07.114</identifier><identifier>PMID: 18671943</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Autoglucosylation ; Autoglucosylation cessation ; Catalysis ; Glucose - metabolism ; Glucosyltransferases - metabolism ; Glycogen - biosynthesis ; Glycogenin ; Glycoproteins - metabolism ; Glycosylation ; Maltose - metabolism ; Polysaccharide-bound glycogenin ; Proteoglycogen ; Rabbits ; Recombinant Proteins - metabolism ; Substrate Specificity</subject><ispartof>Biochemical and biophysical research communications, 2008-10, Vol.374 (4), p.704-708</ispartof><rights>2008 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c354t-878ae0dced7d91523d9a8d5efc6e1b5d53596583933d9b881d832e0a20324803</citedby><cites>FETCH-LOGICAL-c354t-878ae0dced7d91523d9a8d5efc6e1b5d53596583933d9b881d832e0a20324803</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2008.07.114$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18671943$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Romero, Jorge M.</creatorcontrib><creatorcontrib>Issoglio, Federico M.</creatorcontrib><creatorcontrib>Carrizo, María E.</creatorcontrib><creatorcontrib>Curtino, Juan A.</creatorcontrib><title>Evidence for glycogenin autoglucosylation cessation by inaccessibility of the acquired maltosaccharide</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Glycogenin initiates the biosynthesis of proteoglycogen, the mammalian glycogenin-bound glycogen, by intramolecular autoglucosylation. The incubation of glycogenin with UDP-glucose results in formation of a tyrosine-bound maltosaccharide, reaching maximum polymerization degree of 13 glucose units at cessation of the reaction. No exhaustion of the substrate donor occurred at the autoglucosylation end and the full autoglucosylated enzyme continued catalytically active for transglucosylation of the alternative substrate dodecyl-maltose. Even the autoglucosylation cessation once glycogenin acquired a mature maltosaccharide moiety, proteoglycogen and glycogenin species ranging rM 47–200
kDa, derived from proteoglycogen, showed to be autoglucosylable. The results describe for the first time the ability of polysaccharide-bound glycogenin for intramolecular autoglucosylation, providing evidence for cessation of the glucose polymerization initiated into the tyrosine residue, by inaccessibility of the acquired maltosaccharide moiety to further autoglucosylation.</description><subject>Animals</subject><subject>Autoglucosylation</subject><subject>Autoglucosylation cessation</subject><subject>Catalysis</subject><subject>Glucose - metabolism</subject><subject>Glucosyltransferases - metabolism</subject><subject>Glycogen - biosynthesis</subject><subject>Glycogenin</subject><subject>Glycoproteins - metabolism</subject><subject>Glycosylation</subject><subject>Maltose - metabolism</subject><subject>Polysaccharide-bound glycogenin</subject><subject>Proteoglycogen</subject><subject>Rabbits</subject><subject>Recombinant Proteins - metabolism</subject><subject>Substrate Specificity</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMFu3CAURVHVqpkk_YEuKlbd2X0Yg0HqporSpFKkbrLIDmF4njDymATsSP77Ys1I3WUFgnPv0zuEfGVQM2Dyx6Hu--TqBkDV0NWMtR_IjoGGqmHQfiQ7AJBVo9nTBbnM-QBQEKk_kwumZMd0y3dkuH0LHieHdIiJ7sfVxT1OYaJ2meN-XFzM62jnECfqMOfTrV9pmKzbHkIfxjCvNA50fkZq3esSEnp6tOMcc2GebSoDrsmnwY4Zv5zPK_L4-_bx5r56-Hv35-bXQ-W4aOdKdcoieIe-85qJhnttlRc4OImsF15woaVQXPPy0yvFvOINgm2AN60CfkW-n2pfUnxdMM_mGLLDcbQTxiUbqVshJYgCNifQpZhzwsG8pHC0aTUMzCbXHMwm12xyDXSmmCuhb-f2pT-i_x852yzAzxOAZcW3gMlkFza5vjhxs_ExvNf_D3EejS8</recordid><startdate>20081003</startdate><enddate>20081003</enddate><creator>Romero, Jorge M.</creator><creator>Issoglio, Federico M.</creator><creator>Carrizo, María E.</creator><creator>Curtino, Juan A.</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>20081003</creationdate><title>Evidence for glycogenin autoglucosylation cessation by inaccessibility of the acquired maltosaccharide</title><author>Romero, Jorge M. ; Issoglio, Federico M. ; Carrizo, María E. ; Curtino, Juan A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c354t-878ae0dced7d91523d9a8d5efc6e1b5d53596583933d9b881d832e0a20324803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>Autoglucosylation</topic><topic>Autoglucosylation cessation</topic><topic>Catalysis</topic><topic>Glucose - metabolism</topic><topic>Glucosyltransferases - metabolism</topic><topic>Glycogen - biosynthesis</topic><topic>Glycogenin</topic><topic>Glycoproteins - metabolism</topic><topic>Glycosylation</topic><topic>Maltose - metabolism</topic><topic>Polysaccharide-bound glycogenin</topic><topic>Proteoglycogen</topic><topic>Rabbits</topic><topic>Recombinant Proteins - metabolism</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Romero, Jorge M.</creatorcontrib><creatorcontrib>Issoglio, Federico M.</creatorcontrib><creatorcontrib>Carrizo, María E.</creatorcontrib><creatorcontrib>Curtino, Juan A.</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Romero, Jorge M.</au><au>Issoglio, Federico M.</au><au>Carrizo, María E.</au><au>Curtino, Juan A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence for glycogenin autoglucosylation cessation by inaccessibility of the acquired maltosaccharide</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2008-10-03</date><risdate>2008</risdate><volume>374</volume><issue>4</issue><spage>704</spage><epage>708</epage><pages>704-708</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Glycogenin initiates the biosynthesis of proteoglycogen, the mammalian glycogenin-bound glycogen, by intramolecular autoglucosylation. The incubation of glycogenin with UDP-glucose results in formation of a tyrosine-bound maltosaccharide, reaching maximum polymerization degree of 13 glucose units at cessation of the reaction. No exhaustion of the substrate donor occurred at the autoglucosylation end and the full autoglucosylated enzyme continued catalytically active for transglucosylation of the alternative substrate dodecyl-maltose. Even the autoglucosylation cessation once glycogenin acquired a mature maltosaccharide moiety, proteoglycogen and glycogenin species ranging rM 47–200
kDa, derived from proteoglycogen, showed to be autoglucosylable. The results describe for the first time the ability of polysaccharide-bound glycogenin for intramolecular autoglucosylation, providing evidence for cessation of the glucose polymerization initiated into the tyrosine residue, by inaccessibility of the acquired maltosaccharide moiety to further autoglucosylation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18671943</pmid><doi>10.1016/j.bbrc.2008.07.114</doi><tpages>5</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 2008-10, Vol.374 (4), p.704-708 |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Animals Autoglucosylation Autoglucosylation cessation Catalysis Glucose - metabolism Glucosyltransferases - metabolism Glycogen - biosynthesis Glycogenin Glycoproteins - metabolism Glycosylation Maltose - metabolism Polysaccharide-bound glycogenin Proteoglycogen Rabbits Recombinant Proteins - metabolism Substrate Specificity |
| title | Evidence for glycogenin autoglucosylation cessation by inaccessibility of the acquired maltosaccharide |
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