Yeast porphobilinogen deaminase also forms enzyme-pyrrole intermediates
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, parti...
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1994
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10196773_v48_n5-6_p275_Garcia http://hdl.handle.net/20.500.12110/paper_10196773_v48_n5-6_p275_Garcia |
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paper:paper_10196773_v48_n5-6_p275_Garcia |
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paper:paper_10196773_v48_n5-6_p275_Garcia2023-06-08T15:59:54Z Yeast porphobilinogen deaminase also forms enzyme-pyrrole intermediates 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 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. 1994 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10196773_v48_n5-6_p275_Garcia http://hdl.handle.net/20.500.12110/paper_10196773_v48_n5-6_p275_Garcia |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 Yeast porphobilinogen deaminase also forms enzyme-pyrrole intermediates |
| topic_facet |
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 |
| description |
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. |
| title |
Yeast porphobilinogen deaminase also forms enzyme-pyrrole intermediates |
| title_short |
Yeast porphobilinogen deaminase also forms enzyme-pyrrole intermediates |
| title_full |
Yeast porphobilinogen deaminase also forms enzyme-pyrrole intermediates |
| title_fullStr |
Yeast porphobilinogen deaminase also forms enzyme-pyrrole intermediates |
| title_full_unstemmed |
Yeast porphobilinogen deaminase also forms enzyme-pyrrole intermediates |
| title_sort |
yeast porphobilinogen deaminase also forms enzyme-pyrrole intermediates |
| publishDate |
1994 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10196773_v48_n5-6_p275_Garcia http://hdl.handle.net/20.500.12110/paper_10196773_v48_n5-6_p275_Garcia |
| _version_ |
1768544694971662336 |