Involvement of free and enzyme‐bound intermediates in the reaction mechanism catalyzed by the bovine liver immobilized porphobilinogen deaminase. Proof that they are substrates for cosynthetase in uroporphyrinogen III biosynthesis
The detection and accumulation of tetrapyrrole intermediates synthesized by the action of bovine liver porphobilinogen deaminase immobilized to Sepharose 4B is reported. Employing Sepharose‐deaminase preparations, two phases in uroporphyrinogen I synthesis as a function of time were observed, sugges...
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todo:paper_08854513_v13_n2_p173_Kotler2023-10-03T15:40:45Z Involvement of free and enzyme‐bound intermediates in the reaction mechanism catalyzed by the bovine liver immobilized porphobilinogen deaminase. Proof that they are substrates for cosynthetase in uroporphyrinogen III biosynthesis Kotler, M.L. Juknat, A.A. Fumagalli, S.A. Batlle, A.M. immobilized enzyme porphobilinogen deaminase uroporphyrinogen animal article biosynthesis biotechnology cattle enzyme specificity enzymology in vitro study kinetics liver metabolism Animal Biotechnology Cattle Enzymes, Immobilized Hydroxymethylbilane Synthase In Vitro Kinetics Liver Substrate Specificity Support, Non-U.S. Gov't Uroporphyrinogens The detection and accumulation of tetrapyrrole intermediates synthesized by the action of bovine liver porphobilinogen deaminase immobilized to Sepharose 4B is reported. Employing Sepharose‐deaminase preparations, two phases in uroporphyrinogen I synthesis as a function of time were observed, suggesting the accumulation of free and enzyme‐bound intermediates, the concentration and distribution of which were time dependent. The deaminase‐bound intermediate behaves as a substrate in uroporphyrinogen I synthesis whereas the free intermediates produce enzyme inhibition. The tetrapyrrole intermediate bound to the Sepharose‐enzyme is removed from the protein by the binding of porphobilinogen. Free as well as enzyme‐bound intermediates are shown to be substrates for cosynthetase with formation of 80% uroporphyrinogen III. 1991 The Swiss Political Science Review Fil:Kotler, M.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Juknat, A.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Fumagalli, S.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_08854513_v13_n2_p173_Kotler |
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Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
immobilized enzyme porphobilinogen deaminase uroporphyrinogen animal article biosynthesis biotechnology cattle enzyme specificity enzymology in vitro study kinetics liver metabolism Animal Biotechnology Cattle Enzymes, Immobilized Hydroxymethylbilane Synthase In Vitro Kinetics Liver Substrate Specificity Support, Non-U.S. Gov't Uroporphyrinogens |
| spellingShingle |
immobilized enzyme porphobilinogen deaminase uroporphyrinogen animal article biosynthesis biotechnology cattle enzyme specificity enzymology in vitro study kinetics liver metabolism Animal Biotechnology Cattle Enzymes, Immobilized Hydroxymethylbilane Synthase In Vitro Kinetics Liver Substrate Specificity Support, Non-U.S. Gov't Uroporphyrinogens Kotler, M.L. Juknat, A.A. Fumagalli, S.A. Batlle, A.M. Involvement of free and enzyme‐bound intermediates in the reaction mechanism catalyzed by the bovine liver immobilized porphobilinogen deaminase. Proof that they are substrates for cosynthetase in uroporphyrinogen III biosynthesis |
| topic_facet |
immobilized enzyme porphobilinogen deaminase uroporphyrinogen animal article biosynthesis biotechnology cattle enzyme specificity enzymology in vitro study kinetics liver metabolism Animal Biotechnology Cattle Enzymes, Immobilized Hydroxymethylbilane Synthase In Vitro Kinetics Liver Substrate Specificity Support, Non-U.S. Gov't Uroporphyrinogens |
| description |
The detection and accumulation of tetrapyrrole intermediates synthesized by the action of bovine liver porphobilinogen deaminase immobilized to Sepharose 4B is reported. Employing Sepharose‐deaminase preparations, two phases in uroporphyrinogen I synthesis as a function of time were observed, suggesting the accumulation of free and enzyme‐bound intermediates, the concentration and distribution of which were time dependent. The deaminase‐bound intermediate behaves as a substrate in uroporphyrinogen I synthesis whereas the free intermediates produce enzyme inhibition. The tetrapyrrole intermediate bound to the Sepharose‐enzyme is removed from the protein by the binding of porphobilinogen. Free as well as enzyme‐bound intermediates are shown to be substrates for cosynthetase with formation of 80% uroporphyrinogen III. 1991 The Swiss Political Science Review |
| format |
JOUR |
| author |
Kotler, M.L. Juknat, A.A. Fumagalli, S.A. Batlle, A.M. |
| author_facet |
Kotler, M.L. Juknat, A.A. Fumagalli, S.A. Batlle, A.M. |
| author_sort |
Kotler, M.L. |
| title |
Involvement of free and enzyme‐bound intermediates in the reaction mechanism catalyzed by the bovine liver immobilized porphobilinogen deaminase. Proof that they are substrates for cosynthetase in uroporphyrinogen III biosynthesis |
| title_short |
Involvement of free and enzyme‐bound intermediates in the reaction mechanism catalyzed by the bovine liver immobilized porphobilinogen deaminase. Proof that they are substrates for cosynthetase in uroporphyrinogen III biosynthesis |
| title_full |
Involvement of free and enzyme‐bound intermediates in the reaction mechanism catalyzed by the bovine liver immobilized porphobilinogen deaminase. Proof that they are substrates for cosynthetase in uroporphyrinogen III biosynthesis |
| title_fullStr |
Involvement of free and enzyme‐bound intermediates in the reaction mechanism catalyzed by the bovine liver immobilized porphobilinogen deaminase. Proof that they are substrates for cosynthetase in uroporphyrinogen III biosynthesis |
| title_full_unstemmed |
Involvement of free and enzyme‐bound intermediates in the reaction mechanism catalyzed by the bovine liver immobilized porphobilinogen deaminase. Proof that they are substrates for cosynthetase in uroporphyrinogen III biosynthesis |
| title_sort |
involvement of free and enzyme‐bound intermediates in the reaction mechanism catalyzed by the bovine liver immobilized porphobilinogen deaminase. proof that they are substrates for cosynthetase in uroporphyrinogen iii biosynthesis |
| url |
http://hdl.handle.net/20.500.12110/paper_08854513_v13_n2_p173_Kotler |
| work_keys_str_mv |
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1807320791764697088 |