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Yeast Porphobilinogen Deaminase also Forms Enzyme-Pyrrole Intermediates

Yeast Porphobilinogen Deaminase also Forms Enzyme-Pyrrole Intermediates The enzyme porphobilinogen deaminase (PBG deaminase. EC 4.3.1.8) catalyzesthe 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 orpresence of phenylmethylsulfonyl fluoride (PMSF) and preincubated with PBG. was appliedon DEAE-cellulose columns, three peaks with PBG deaminase activity were detected.Using Ehrlich’s reagent, it was found that the active peaks corresponded tomono-, di- and tri-pyrrylmethane-enzyme complexes. Therefore, the mechanism of actionof PBG deaminase from Saccharomyces cerevisiae also involves the sequential additionof four PBG units, leading to the formation of the enzyme-substrate intermediatecomplexes, as has already been described for the same enzyme from other sources. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Enzyme and Protein Karger

Yeast Porphobilinogen Deaminase also Forms Enzyme-Pyrrole Intermediates

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Publisher
Karger
Copyright
© 1994 S. Karger AG, Basel
ISSN
1019-6773
eISSN
2504-2556
DOI
10.1159/000475000
Publisher site
See Article on Publisher Site

Abstract

The enzyme porphobilinogen deaminase (PBG deaminase. EC 4.3.1.8) catalyzesthe 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 orpresence of phenylmethylsulfonyl fluoride (PMSF) and preincubated with PBG. was appliedon DEAE-cellulose columns, three peaks with PBG deaminase activity were detected.Using Ehrlich’s reagent, it was found that the active peaks corresponded tomono-, di- and tri-pyrrylmethane-enzyme complexes. Therefore, the mechanism of actionof PBG deaminase from Saccharomyces cerevisiae also involves the sequential additionof four PBG units, leading to the formation of the enzyme-substrate intermediatecomplexes, as has already been described for the same enzyme from other sources.

Journal

Enzyme and Protein – Karger

Published: Jan 1, 2017

Keywords: Porphobilinogen; Porphobilinogen deaminase; Saccharomyces cerevisiae; Substrate-enzyme complexes

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