Vitali A, Botta B, Delle Monache G, Zappitelli S, Ricciardi P, Melino S, Petruzzelli R, Giardina B
C.N.R. Centro Chimica dei Recettori e delle Molecole Biologicamente Attive, Istituto di Chimica e Chimica Clinica, Facoltà di Medicina e Chirurgia, Università Cattolica S. Cuore, L.go F. Vito 1, 00168 Roma, Italy.
Biochem J. 1998 Apr 15;331 ( Pt 2)(Pt 2):513-9. doi: 10.1042/bj3310513.
An acidic peroxidase (EC 1.11.1.7) produced by cell suspension cultures of Cassia didymobotrya (wild senna) was purified from culture medium collected on the 29th day. The enzyme was shown to be a glycoprotein with a pI of 3.5, a molecular mass of approx. 43 kDa by SDS/PAGE and 50 kDa by gel filtration. The N-terminal sequence was very similar to those of other plant peroxidases. The peroxidase was characterized by a high specificity towards coniferyl alcohol and other natural phenolics such as guaiacol and ferulic and caffeic acids. These findings suggest that the enzyme is involved in lignification processes of the cell wall. Moreover, the enzyme was able to catalyse the oxidation of 4,3',4'-trihydroxychalcone and 4, 3',4'-trihydroxy-3-methoxychalcone to the corresponding 3, 3'-biflavanones, as mixtures of racemic and meso forms.
从第29天收集的培养基中纯化出由双荚决明(野生番泻叶)细胞悬浮培养物产生的一种酸性过氧化物酶(EC 1.11.1.7)。该酶被证明是一种糖蛋白,其pI为3.5,通过SDS/PAGE测得分子量约为43 kDa,通过凝胶过滤测得分子量为50 kDa。其N端序列与其他植物过氧化物酶的序列非常相似。该过氧化物酶对松柏醇和其他天然酚类物质(如愈创木酚、阿魏酸和咖啡酸)具有高度特异性。这些发现表明该酶参与细胞壁的木质化过程。此外,该酶能够将4,3',4'-三羟基查耳酮和4,3',4'-三羟基-3-甲氧基查耳酮催化氧化为相应的3,3'-双黄酮,以外消旋体和内消旋体形式的混合物存在。