Artículo
Abstract:
The enzyme porphobilinogen deaminase (PEG deaminase, EC 4.3.1.8) catalyzes the condensation of four molecules of PBG to give the linear tetrapyrrol, hydroxymethylbilane. It has been shown that this enzyme forms stable mono-, di-, tri- and tetrapyrrol-enzyme covalent complexes. When the enzyme, partially purified in the absence or presence of phenylmethylsulfonyl fluoride (PMSF) and preincubated with PBG, was applied on DEAE-cellulose columns, three peaks with PBG deaminase activity were detected. Using Ehrlich's reagent, it was found that the active peaks corresponded to mono-, di- and tri-pyrrylmethane-enzyme complexes. Therefore, the mechanism of action of PBG deaminase from Saccharomyces cerevisiae also involves the sequential addition of four PBG units, leading to the formation of the enzyme-substrate intermediate complexes, as has already been described for the same enzyme from other sources.
Registro:
| Documento: | Artículo |
| Título: | Yeast porphobilinogen deaminase also forms enzyme-pyrrole intermediates |
| Autor: | Garcia, S.C.; Rossetti, M.V.; Moretti, M.B.; Del Carmen Batlle, A.M. |
| Filiación: | Centro Invest Porfirinas y Porfirias, CIPYP (CONICET, FCE y N, UBA), Ciudad Universitaria, Buenos Aires, Argentina |
| Palabras clave: | Porphobilinogen; Porphobilinogen deaminase; Saccharomyces cerevisiae; Substrate-enzyme complexes; 4 dimethylaminobenzaldehyde; benzylsulfonyl fluoride; diethylaminoethyl cellulose; porphobilinogen deaminase; pyrrole; article; enzyme activity; enzyme purification; enzyme substrate complex; nonhuman; Saccharomyces cerevisiae; yeast |
| Año: | 1994 |
| Volumen: | 48 |
| Número: | 5-6 |
| Página de inicio: | 275 |
| Página de fin: | 281 |
| DOI: | http://dx.doi.org/10.1159/000475000 |
| Título revista: | Enzyme and Protein |
| Título revista abreviado: | ENZYME PROTEIN |
| ISSN: | 10196773 |
| CODEN: | EPROE |
| CAS: | 4 dimethylaminobenzaldehyde, 100-10-7, 28602-27-9; benzylsulfonyl fluoride, 329-98-6; diethylaminoethyl cellulose, 9013-34-7; porphobilinogen deaminase, 9036-47-9, 9074-91-3; pyrrole, 109-97-7 |
| Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10196773_v48_n5-6_p275_Garcia |
Citas:
---------- APA ----------
Garcia, S.C., Rossetti, M.V., Moretti, M.B. & Del Carmen Batlle, A.M. (1994) . Yeast porphobilinogen deaminase also forms enzyme-pyrrole intermediates. Enzyme and Protein, 48(5-6), 275-281.http://dx.doi.org/10.1159/000475000
---------- CHICAGO ----------
Garcia, S.C., Rossetti, M.V., Moretti, M.B., Del Carmen Batlle, A.M. "Yeast porphobilinogen deaminase also forms enzyme-pyrrole intermediates" . Enzyme and Protein 48, no. 5-6 (1994) : 275-281.http://dx.doi.org/10.1159/000475000
---------- MLA ----------
Garcia, S.C., Rossetti, M.V., Moretti, M.B., Del Carmen Batlle, A.M. "Yeast porphobilinogen deaminase also forms enzyme-pyrrole intermediates" . Enzyme and Protein, vol. 48, no. 5-6, 1994, pp. 275-281.http://dx.doi.org/10.1159/000475000
---------- VANCOUVER ----------
Garcia, S.C., Rossetti, M.V., Moretti, M.B., Del Carmen Batlle, A.M. Yeast porphobilinogen deaminase also forms enzyme-pyrrole intermediates. ENZYME PROTEIN. 1994;48(5-6):275-281.http://dx.doi.org/10.1159/000475000
