{"id":{"repo_id":"vt","oai_identifier":"oai:vtechworks.lib.vt.edu:10919/41960"},"canonical_url":"https://search.dev.ndltd.org/etd/vt/oai:vtechworks.lib.vt.edu:10919/41960","repository":{"repo_id":"vt","name":"Virginia Tech","base_url":"https://vtechworks.lib.vt.edu/oai/request"},"display":{"title":"Studies on some enzymatic properties of mitochondrial propionyl carboxylase","abstract":"Propionyl carboxylase purified from bovine liver mitochondria catalyzes the carboxylation of 992 micromoles of propionyl-CoA per hour per milligram of protein. Relative carboxylation rates for acetyl-, propionyl-, butyryl-, and valeryl-CoA remain constant during purification. The carboxylase is inhibited by PCMB, N-ethylmaleimide, and iodoacetamide; and the inhibition by PCMB can be almost completely reversed by GSH. The K<sub>m</sub> values for acetyl-CoA, propionyl-CoA, butyryl-CoA, valeryh-CoA, propionyl pantetheine, ATP, and HCOj were determined. The K<sub>m</sub> values for the aeyl-CoA derivatives are approximately the same while there is a 200-fold difference between the V<sub>m</sub> values for propionyl-CoA and valeryl-CoA. Coenzyme A and valeryl-CoA, but not propionyl pantetheine were found to be competitive inhibitors of propionyl carboxylase. The apparent equilibrium constant for the enzymatic propionyl-CoA carboxylation reaction at pH 8.15 and 37°c is 8.1 x 10<sup>-3</sup> and the Δ F°<sub>310</sub> calculated from this constant is 2970 calories per mole.","abstract_html":"Propionyl carboxylase purified from bovine liver mitochondria catalyzes the carboxylation of 992 micromoles of propionyl-CoA per hour per milligram of protein. Relative carboxylation rates for acetyl-, propionyl-, butyryl-, and valeryl-CoA remain constant during purification. The carboxylase is inhibited by PCMB, N-ethylmaleimide, and iodoacetamide; and the inhibition by PCMB can be almost completely reversed by GSH. The K&lt;sub&gt;m&lt;/sub&gt; values for acetyl-CoA, propionyl-CoA, butyryl-CoA, valeryh-CoA, propionyl pantetheine, ATP, and HCOj were determined. The K&lt;sub&gt;m&lt;/sub&gt; values for the aeyl-CoA derivatives are approximately the same while there is a 200-fold difference between the V&lt;sub&gt;m&lt;/sub&gt; values for propionyl-CoA and valeryl-CoA. Coenzyme A and valeryl-CoA, but not propionyl pantetheine were found to be competitive inhibitors of propionyl carboxylase. The apparent equilibrium constant for the enzymatic propionyl-CoA carboxylation reaction at pH 8.15 and 37°c is 8.1 x 10&lt;sup&gt;-3&lt;/sup&gt; and the Δ F°&lt;sub&gt;310&lt;/sub&gt; calculated from this constant is 2970 calories per mole.","abstract_has_math":false,"creators":["Feng, Marjorie Jan-yung"],"institution":"Virginia Tech","degree_name":"Master of Science","degree_level":"masters","degree_discipline":"Biochemistry and Nutrition","degree_department":"Biochemistry and Nutrition","school":null,"contributors":[],"advisors":[],"committee_chairs":["Lane, M. Daniel"],"committee_members":["Engel, R. W.","King, Kendall W.","Vingiello, Frank A."],"year":1962,"date_issued":"1962-05-05","date_published":"1962-05-05","updated_at":"2026-07-22T22:19:29Z","subjects":[],"languages":[],"rights":["In Copyright"],"rights_urls":["http://rightsstatements.org/vocab/InC/1.0/"],"identifier_entries":[{"key":"dc:identifier.other","label":"Dc Identifier Other","values":["etd-04072010-020058"],"render_values":[{"text":"etd-04072010-020058","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/10919/41960","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.committeechair","label":"Committee Chair","values":["Lane, M. Daniel"]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Engel, R. 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Relative carboxylation rates for acetyl-, propionyl-, butyryl-, and valeryl-CoA remain constant during purification. The carboxylase is inhibited by PCMB, N-ethylmaleimide, and iodoacetamide; and the inhibition by PCMB can be almost completely reversed by GSH. The K<sub>m</sub> values for acetyl-CoA, propionyl-CoA, butyryl-CoA, valeryh-CoA, propionyl pantetheine, ATP, and HCOj were determined. The K<sub>m</sub> values for the aeyl-CoA derivatives are approximately the same while there is a 200-fold difference between the V<sub>m</sub> values for propionyl-CoA and valeryl-CoA. Coenzyme A and valeryl-CoA, but not propionyl pantetheine were found to be competitive inhibitors of propionyl carboxylase. The apparent equilibrium constant for the enzymatic propionyl-CoA carboxylation reaction at pH 8.15 and 37°c is 8.1 x 10<sup>-3</sup> and the Δ F°<sub>310</sub> calculated from this constant is 2970 calories per mole."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["Master of Science"]},{"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":["Studies on some enzymatic properties of mitochondrial propionyl carboxylase"]}]}],"canonical_facts":{"dc:contributor.committeechair":["Lane, M. Daniel"],"dc:contributor.committeemember":["Engel, R. W.","King, Kendall W.","Vingiello, Frank A."],"dc:contributor.department":["Biochemistry and Nutrition"],"dc:creator":["Feng, Marjorie Jan-yung"],"dc:date.accessioned":["2014-03-14T21:33:10Z"],"dc:date.available":["2014-03-14T21:33:10Z","2010-04-07"],"dc:date.issued":["1962-05-05"],"dc:description.abstract":["Propionyl carboxylase purified from bovine liver mitochondria catalyzes the carboxylation of 992 micromoles of propionyl-CoA per hour per milligram of protein. Relative carboxylation rates for acetyl-, propionyl-, butyryl-, and valeryl-CoA remain constant during purification. The carboxylase is inhibited by PCMB, N-ethylmaleimide, and iodoacetamide; and the inhibition by PCMB can be almost completely reversed by GSH. The K<sub>m</sub> values for acetyl-CoA, propionyl-CoA, butyryl-CoA, valeryh-CoA, propionyl pantetheine, ATP, and HCOj were determined. The K<sub>m</sub> values for the aeyl-CoA derivatives are approximately the same while there is a 200-fold difference between the V<sub>m</sub> values for propionyl-CoA and valeryl-CoA. Coenzyme A and valeryl-CoA, but not propionyl pantetheine were found to be competitive inhibitors of propionyl carboxylase. The apparent equilibrium constant for the enzymatic propionyl-CoA carboxylation reaction at pH 8.15 and 37°c is 8.1 x 10<sup>-3</sup> and the Δ F°<sub>310</sub> calculated from this constant is 2970 calories per mole."],"dc:description.degree":["Master of Science"],"dc:format.medium":["BTD"],"dc:format.mimetype":["application/pdf"],"dc:identifier.other":["etd-04072010-020058"],"dc:identifier.uri":["http://hdl.handle.net/10919/41960"],"dc:publisher":["Virginia Tech"],"dc:rights":["In Copyright"],"dc:rights.uri":["http://rightsstatements.org/vocab/InC/1.0/"],"dc:title":["Studies on some enzymatic properties of mitochondrial propionyl carboxylase"],"dc:type":["Thesis"],"dc:type.dcmitype":["Text"],"thesis:degree_discipline":["Biochemistry and Nutrition"],"thesis:degree_level":["masters"],"thesis:degree_name":["Master of Science"],"thesis:institution_name":["Virginia Polytechnic Institute"]},"updated_at":"2026-07-22T22:19:29Z"}