{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/95627"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/95627","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Biochemical characterization of five GH130-family enzymes from Caldanaerobius polysaccharolyticus ATCC BAA-17 and insights on their metabolic role and reaction mechanisms","abstract":"Proteins in the glycoside hydrolase family 130 (GH130, CAZy database) have been proposed to perform the phosphorolysis of β-1,2 and β-1,4-mannosyl linkages between the mannose at the non-reducing end of substrates and mannose, glucose or N-acetylglucosamine residues, with the subsequent release of α-mannose-1-phosphate. In this study, we compare five different GH130 enzymes (CpMan130 A-E) encoded within the genome of Caldanaerobius polysaccharolyticus, a thermophilic anaerobic bacterium able to ferment mannan as the sole carbon source. Analysis of substrate specificity and end product release allowed for the identification of pathways involving GH130 enzymes in the metabolism of mannans with different structures by this organism. Mechanistic studies involving the binding order and amino acid mapping on a three-dimensional model of Man130B helped to elucidate the ordered sequential bi-bi mechanism utilized by these enzymes. Phylogenetic analysis of over 950 sequences assigned to the GH130 family, combined with differences in amino acid conservation and substrate specificity, revealed a new subgroup for this family, GH130_3, consisting of thermostable enzymes that act on β-1,2-linked manno-oligosaccharides. The genomic context of all genes in the proposed subgroup GH130_3 suggests that they appear in pairs, preceded by an ABC-like transporter.","abstract_html":"Proteins in the glycoside hydrolase family 130 (GH130, CAZy database) have been proposed to perform the phosphorolysis of β-1,2 and β-1,4-mannosyl linkages between the mannose at the non-reducing end of substrates and mannose, glucose or N-acetylglucosamine residues, with the subsequent release of α-mannose-1-phosphate. In this study, we compare five different GH130 enzymes (CpMan130 A-E) encoded within the genome of Caldanaerobius polysaccharolyticus, a thermophilic anaerobic bacterium able to ferment mannan as the sole carbon source. Analysis of substrate specificity and end product release allowed for the identification of pathways involving GH130 enzymes in the metabolism of mannans with different structures by this organism. Mechanistic studies involving the binding order and amino acid mapping on a three-dimensional model of Man130B helped to elucidate the ordered sequential bi-bi mechanism utilized by these enzymes. Phylogenetic analysis of over 950 sequences assigned to the GH130 family, combined with differences in amino acid conservation and substrate specificity, revealed a new subgroup for this family, GH130_3, consisting of thermostable enzymes that act on β-1,2-linked manno-oligosaccharides. The genomic context of all genes in the proposed subgroup GH130_3 suggests that they appear in pairs, preceded by an ABC-like transporter.","abstract_has_math":false,"creators":["Muller Paul, Hans M"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"M.S.","degree_level":"Thesis","degree_discipline":"Animal Sciences","degree_department":null,"school":null,"contributors":["Cann, Isaac"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2017,"date_issued":"2017-03-01T17:02:12Z","date_published":"2017-03-01T17:02:12Z","updated_at":"2026-07-22T22:26:37Z","subjects":["GH130","Enzyme","Phosphorolysis","Mannan","Thermophilic"],"languages":["en"],"rights":["Copyright 2016 Hans Muller Paul"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/2142/95627","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Cann, Isaac"]},{"key":"dc:creator","label":"Author","values":["Muller Paul, Hans M"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2017-03-01T17:02:12Z","2019-03-02T10:15:24Z","2016-12-09","2016-12"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Animal Sciences"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["M.S."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["GH130","Enzyme","Phosphorolysis","Mannan","Thermophilic"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 2016 Hans Muller Paul"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/95627"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Proteins in the glycoside hydrolase family 130 (GH130, CAZy database) have been proposed to perform the phosphorolysis of β-1,2 and β-1,4-mannosyl linkages between the mannose at the non-reducing end of substrates and mannose, glucose or N-acetylglucosamine residues, with the subsequent release of α-mannose-1-phosphate. In this study, we compare five different GH130 enzymes (CpMan130 A-E) encoded within the genome of Caldanaerobius polysaccharolyticus, a thermophilic anaerobic bacterium able to ferment mannan as the sole carbon source. Analysis of substrate specificity and end product release allowed for the identification of pathways involving GH130 enzymes in the metabolism of mannans with different structures by this organism. Mechanistic studies involving the binding order and amino acid mapping on a three-dimensional model of Man130B helped to elucidate the ordered sequential bi-bi mechanism utilized by these enzymes. Phylogenetic analysis of over 950 sequences assigned to the GH130 family, combined with differences in amino acid conservation and substrate specificity, revealed a new subgroup for this family, GH130_3, consisting of thermostable enzymes that act on β-1,2-linked manno-oligosaccharides. The genomic context of all genes in the proposed subgroup GH130_3 suggests that they appear in pairs, preceded by an ABC-like transporter.","Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2018-12-01","The student, Hans Muller Paul, accepted the attached license on 2016-12-09 at 14:59.","The student, Hans Muller Paul, submitted this Thesis for approval on 2016-12-09 at 15:16.","This Thesis was approved for publication on 2016-12-09 at 16:32.","DSpace SAF Submission Ingestion Package generated from Vireo submission #10501 on 2017-02-28 at 14:43:38","Made available in DSpace on 2017-03-01T17:02:12Z (GMT). No. of bitstreams: 2 MULLERPAUL-THESIS-2016.pdf: 10626788 bytes, checksum: 562810c4c8a8a8ca01d3689ae9117214 (MD5) LICENSE.txt: 4213 bytes, checksum: f4bf83636f9d8d1aba3cae2d1319f43a (MD5) Previous issue date: 2016-12-09","Embargo set by: Seth Robbins for item 98743 Lift date: 2019-03-01T17:02:22Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","Embargo set by: Seth Robbins for item 98743 Lift date: 2019-03-01T17:03:32Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","Embargo set by: Seth Robbins for item 98743 Lift date: 2019-03-01T17:05:02Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","Embargo set by: Seth Robbins for item 98743 Lift date: 2019-03-01T17:06:55Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","Limited Restriction Lifted for Item 98743 on 2019-03-02T10:15:24Z."]},{"key":"dc:format","label":"Dc Format","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Biochemical characterization of five GH130-family enzymes from Caldanaerobius polysaccharolyticus ATCC BAA-17 and insights on their metabolic role and reaction mechanisms"]}]}],"canonical_facts":{"dc:contributor":["Cann, Isaac"],"dc:creator":["Muller Paul, Hans M"],"dc:date":["2017-03-01T17:02:12Z","2019-03-02T10:15:24Z","2016-12-09","2016-12"],"dc:description":["Proteins in the glycoside hydrolase family 130 (GH130, CAZy database) have been proposed to perform the phosphorolysis of β-1,2 and β-1,4-mannosyl linkages between the mannose at the non-reducing end of substrates and mannose, glucose or N-acetylglucosamine residues, with the subsequent release of α-mannose-1-phosphate. In this study, we compare five different GH130 enzymes (CpMan130 A-E) encoded within the genome of Caldanaerobius polysaccharolyticus, a thermophilic anaerobic bacterium able to ferment mannan as the sole carbon source. Analysis of substrate specificity and end product release allowed for the identification of pathways involving GH130 enzymes in the metabolism of mannans with different structures by this organism. Mechanistic studies involving the binding order and amino acid mapping on a three-dimensional model of Man130B helped to elucidate the ordered sequential bi-bi mechanism utilized by these enzymes. Phylogenetic analysis of over 950 sequences assigned to the GH130 family, combined with differences in amino acid conservation and substrate specificity, revealed a new subgroup for this family, GH130_3, consisting of thermostable enzymes that act on β-1,2-linked manno-oligosaccharides. The genomic context of all genes in the proposed subgroup GH130_3 suggests that they appear in pairs, preceded by an ABC-like transporter.","Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2018-12-01","The student, Hans Muller Paul, accepted the attached license on 2016-12-09 at 14:59.","The student, Hans Muller Paul, submitted this Thesis for approval on 2016-12-09 at 15:16.","This Thesis was approved for publication on 2016-12-09 at 16:32.","DSpace SAF Submission Ingestion Package generated from Vireo submission #10501 on 2017-02-28 at 14:43:38","Made available in DSpace on 2017-03-01T17:02:12Z (GMT). No. of bitstreams: 2 MULLERPAUL-THESIS-2016.pdf: 10626788 bytes, checksum: 562810c4c8a8a8ca01d3689ae9117214 (MD5) LICENSE.txt: 4213 bytes, checksum: f4bf83636f9d8d1aba3cae2d1319f43a (MD5) Previous issue date: 2016-12-09","Embargo set by: Seth Robbins for item 98743 Lift date: 2019-03-01T17:02:22Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","Embargo set by: Seth Robbins for item 98743 Lift date: 2019-03-01T17:03:32Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","Embargo set by: Seth Robbins for item 98743 Lift date: 2019-03-01T17:05:02Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","Embargo set by: Seth Robbins for item 98743 Lift date: 2019-03-01T17:06:55Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","Limited Restriction Lifted for Item 98743 on 2019-03-02T10:15:24Z."],"dc:format":["application/pdf"],"dc:identifier":["http://hdl.handle.net/2142/95627"],"dc:language":["en"],"dc:rights":["Copyright 2016 Hans Muller Paul"],"dc:subject":["GH130","Enzyme","Phosphorolysis","Mannan","Thermophilic"],"dc:title":["Biochemical characterization of five GH130-family enzymes from Caldanaerobius polysaccharolyticus ATCC BAA-17 and insights on their metabolic role and reaction mechanisms"],"dc:type":["text"],"thesis:degree_discipline":["Animal Sciences"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["M.S."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:37Z"}