Correa Garcia S, Rossetti M V, Bermudez Moretti M, Batlle A M
Centro de Investigaciones sobre Porfirinas y Porfirias, CIPYP (CONICET, FCE y N, UBA), Ciudad Universitaria, Buenos Aires, Argentina.
Enzyme Protein. 1994;48(5-6):275-81. doi: 10.1159/000475000.
The enzyme porphobilinogen deaminase (PBG 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 tetrapyrrole-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.
胆色素原脱氨酶（PBG脱氨酶，EC 4.3.1.8）催化四分子胆色素原缩合生成线性四吡咯——羟甲基胆色素。已表明该酶能形成稳定的单吡咯、二吡咯、三吡咯和四吡咯-酶共价复合物。当在不存在或存在苯甲基磺酰氟（PMSF）的情况下部分纯化该酶，并与胆色素原预孵育后，将其应用于DEAE-纤维素柱时，检测到三个具有胆色素原脱氨酶活性的峰。使用埃利希试剂发现，活性峰对应于单吡咯甲烷-酶复合物、二吡咯甲烷-酶复合物和三吡咯甲烷-酶复合物。因此，酿酒酵母的胆色素原脱氨酶的作用机制也涉及依次添加四个胆色素原单元，导致形成酶-底物中间复合物，这与已报道的来自其他来源的同一种酶的情况相同。
