{"id":{"repo_id":"vt","oai_identifier":"oai:vtechworks.lib.vt.edu:10919/38486"},"canonical_url":"https://search.dev.ndltd.org/etd/vt/oai:vtechworks.lib.vt.edu:10919/38486","repository":{"repo_id":"vt","name":"Virginia Tech","base_url":"https://vtechworks.lib.vt.edu/oai/request"},"display":{"title":"Carbonic anhydrase from Methanosarcina thermophila: proposal of a new class of carbonic anhydrases and putative roles for the enzyme in anaerobic acetate catabolism","abstract":"Carbonic anhydrase (CA) from acetate-grown Methanosarcina thermophila strain TM-1 was purified> 10,OOO-fold (22% recovery) to apparent homogeneity and a specific activity of 4,900 units mg⁻¹.The gene encoding this CA was isolated fronl a partial genomic library on a 12-kb fragment and sequenced. Comparison of the deduced anlino acid sequence with the N-terminaI sequence of the purified protein shows that the gene encodes an additional 34 N-terminal residues with properties characteristic of signal peptides in secretory proteins. The deduced amino acid sequence has no significant identity to any known CAs, but has, among others, 35% sequence identity to the first 197 deduced N-terminal amino acids of a proposed CO₂-concentrating-mechanism protein from <i>Synechococcus</i> sp. strain PCC7942.","abstract_html":"Carbonic anhydrase (CA) from acetate-grown Methanosarcina thermophila strain TM-1 was purified&gt; 10,OOO-fold (22% recovery) to apparent homogeneity and a specific activity of 4,900 units mg⁻¹.The gene encoding this CA was isolated fronl a partial genomic library on a 12-kb fragment and sequenced. Comparison of the deduced anlino acid sequence with the N-terminaI sequence of the purified protein shows that the gene encodes an additional 34 N-terminal residues with properties characteristic of signal peptides in secretory proteins. The deduced amino acid sequence has no significant identity to any known CAs, but has, among others, 35% sequence identity to the first 197 deduced N-terminal amino acids of a proposed CO₂-concentrating-mechanism protein from &lt;i&gt;Synechococcus&lt;/i&gt; sp. strain PCC7942.","abstract_has_math":false,"creators":["Alber, Birgit E."],"institution":"Virginia Tech","degree_name":"Ph. D.","degree_level":"doctoral","degree_discipline":"Biochemistry and Anaerobic Microbiology","degree_department":"Biochemistry and Anaerobic Microbiology","school":null,"contributors":[],"advisors":[],"committee_chairs":["Ferry, James G."],"committee_members":["Dean, Dennis R.","Johnson, John L.","Gregory, Eugene M.","Niehaus, Walter G. Jr."],"year":1995,"date_issued":"1995-06-09","date_published":"1995-06-09","updated_at":"2026-07-22T22:18:44Z","subjects":["carbonic anhydrase","CA"],"languages":["en"],"rights":["In Copyright"],"rights_urls":["http://rightsstatements.org/vocab/InC/1.0/"],"identifier_entries":[{"key":"dc:identifier.other","label":"Dc Identifier Other","values":["etd-06062008-171625"],"render_values":[{"text":"etd-06062008-171625","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/10919/38486","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.committeechair","label":"Committee Chair","values":["Ferry, James G."]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Dean, Dennis R.","Johnson, John L.","Gregory, Eugene M.","Niehaus, Walter G. Jr."]},{"key":"dc:contributor.department","label":"Department","values":["Biochemistry and Anaerobic Microbiology"]},{"key":"dc:creator","label":"Author","values":["Alber, Birgit E."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2014-03-14T21:14:34Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2014-03-14T21:14:34Z","2008-06-06"]},{"key":"dc:date.issued","label":"Date","values":["1995-06-09"]},{"key":"dc:publisher","label":"Institution","values":["Virginia Tech"]},{"key":"dc:type","label":"Dc Type","values":["Dissertation"]},{"key":"dc:type.dcmitype","label":"Dc Type Dcmitype","values":["Text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry and Anaerobic Microbiology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["doctoral"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph. D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Virginia Polytechnic Institute and State University"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["carbonic anhydrase","CA"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["In Copyright"]},{"key":"dc:rights.uri","label":"Rights URI","values":["http://rightsstatements.org/vocab/InC/1.0/"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.other","label":"Dc Identifier Other","values":["etd-06062008-171625"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/10919/38486"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Carbonic anhydrase (CA) from acetate-grown Methanosarcina thermophila strain TM-1 was purified> 10,OOO-fold (22% recovery) to apparent homogeneity and a specific activity of 4,900 units mg⁻¹.The gene encoding this CA was isolated fronl a partial genomic library on a 12-kb fragment and sequenced. Comparison of the deduced anlino acid sequence with the N-terminaI sequence of the purified protein shows that the gene encodes an additional 34 N-terminal residues with properties characteristic of signal peptides in secretory proteins. The deduced amino acid sequence has no significant identity to any known CAs, but has, among others, 35% sequence identity to the first 197 deduced N-terminal amino acids of a proposed CO₂-concentrating-mechanism protein from <i>Synechococcus</i> sp. strain PCC7942."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["Ph. D."]},{"key":"dc:format.medium","label":"Dc Format Medium","values":["BTD"]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Carbonic anhydrase from Methanosarcina thermophila: proposal of a new class of carbonic anhydrases and putative roles for the enzyme in anaerobic acetate catabolism"]}]}],"canonical_facts":{"dc:contributor.committeechair":["Ferry, James G."],"dc:contributor.committeemember":["Dean, Dennis R.","Johnson, John L.","Gregory, Eugene M.","Niehaus, Walter G. Jr."],"dc:contributor.department":["Biochemistry and Anaerobic Microbiology"],"dc:creator":["Alber, Birgit E."],"dc:date.accessioned":["2014-03-14T21:14:34Z"],"dc:date.available":["2014-03-14T21:14:34Z","2008-06-06"],"dc:date.issued":["1995-06-09"],"dc:description.abstract":["Carbonic anhydrase (CA) from acetate-grown Methanosarcina thermophila strain TM-1 was purified> 10,OOO-fold (22% recovery) to apparent homogeneity and a specific activity of 4,900 units mg⁻¹.The gene encoding this CA was isolated fronl a partial genomic library on a 12-kb fragment and sequenced. Comparison of the deduced anlino acid sequence with the N-terminaI sequence of the purified protein shows that the gene encodes an additional 34 N-terminal residues with properties characteristic of signal peptides in secretory proteins. The deduced amino acid sequence has no significant identity to any known CAs, but has, among others, 35% sequence identity to the first 197 deduced N-terminal amino acids of a proposed CO₂-concentrating-mechanism protein from <i>Synechococcus</i> sp. strain PCC7942."],"dc:description.degree":["Ph. D."],"dc:format.medium":["BTD"],"dc:format.mimetype":["application/pdf"],"dc:identifier.other":["etd-06062008-171625"],"dc:identifier.uri":["http://hdl.handle.net/10919/38486"],"dc:language.iso":["en"],"dc:publisher":["Virginia Tech"],"dc:rights":["In Copyright"],"dc:rights.uri":["http://rightsstatements.org/vocab/InC/1.0/"],"dc:subject":["carbonic anhydrase","CA"],"dc:title":["Carbonic anhydrase from Methanosarcina thermophila: proposal of a new class of carbonic anhydrases and putative roles for the enzyme in anaerobic acetate catabolism"],"dc:type":["Dissertation"],"dc:type.dcmitype":["Text"],"thesis:degree_discipline":["Biochemistry and Anaerobic Microbiology"],"thesis:degree_level":["doctoral"],"thesis:degree_name":["Ph. D."],"thesis:institution_name":["Virginia Polytechnic Institute and State University"]},"updated_at":"2026-07-22T22:18:44Z"}