Artículo
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" (1991) Biotechnology and Applied Biochemistry. 13(2):173-180
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Abstract:
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
Registro:
| Documento: | Artículo |
| Título: | 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 |
| Autor: | Kotler, M.L.; Juknat, A.A.; Fumagalli, S.A.; Batlle, A.M. |
| Filiación: | Centro de Investigaciones sobre Porfirinas y Porfirias, CIPYP (FCEN, UBA-CONICET), Ciudad Universitaria, Buenos Aires, Argentina |
| Palabras clave: | 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 |
| Año: | 1991 |
| Volumen: | 13 |
| Número: | 2 |
| Página de inicio: | 173 |
| Página de fin: | 180 |
| DOI: | http://dx.doi.org/10.1111/j.1470-8744.1991.tb00150.x |
| Título revista: | Biotechnology and Applied Biochemistry |
| Título revista abreviado: | Biotechnol. Appl. Biochem. |
| ISSN: | 08854513 |
| CAS: | porphobilinogen deaminase, 9036-47-9, 9074-91-3; uroporphyrinogen, 35465-57-7; Enzymes, Immobilized; Hydroxymethylbilane Synthase, EC 4.3.1.8; Uroporphyrinogens |
| Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08854513_v13_n2_p173_Kotler |
Citas:
---------- APA ----------
Kotler, M.L., Juknat, A.A., Fumagalli, S.A. & Batlle, A.M. (1991) . 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. Biotechnology and Applied Biochemistry, 13(2), 173-180.http://dx.doi.org/10.1111/j.1470-8744.1991.tb00150.x
---------- CHICAGO ----------
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" . Biotechnology and Applied Biochemistry 13, no. 2 (1991) : 173-180.http://dx.doi.org/10.1111/j.1470-8744.1991.tb00150.x
---------- MLA ----------
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" . Biotechnology and Applied Biochemistry, vol. 13, no. 2, 1991, pp. 173-180.http://dx.doi.org/10.1111/j.1470-8744.1991.tb00150.x
---------- VANCOUVER ----------
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. Biotechnol. Appl. Biochem. 1991;13(2):173-180.http://dx.doi.org/10.1111/j.1470-8744.1991.tb00150.x
