Niemetz Ruth, Gross Georg G
Molekulare Botanik, Universität Ulm, D-89069 Ulm, Germany.
Phytochemistry. 2003 Dec;64(7):1197-201. doi: 10.1016/j.phytochem.2003.08.013.
An enzyme has been purified from leaves of the weed Tellima grandiflora (fringe cups, Saxifragaceae) that catalyzed the O2-dependent oxidation of the monomeric ellagitannin, tellimagrandin II, to a dimeric derivative, cornusiin E. The apparently homogeneous enzyme preparation had a Mr of ca. 160,000 (with four subunits of Mr 40,000), a pH-optimum and an isoelectric point at pH 5.2, and was most stable at pH 4.3. Inhibition studies revealed that this new enzyme, for which the systematic name 'tellimagrandin II: O2 oxidoreductase' is proposed, is a member of the laccase (EC 1.10.3.2) family of phenol oxidases. The properties of this enzyme differed from that of a related laccase that catalyzed the transition of 1,2,3,4,6-pentagalloylglucopyranose to tellimagrandin II, the preceding step in the biosynthetic route to cornusin E.
从野草大花Tellima(虎耳草科,流苏杯草)的叶子中纯化出一种酶,该酶催化单体鞣花单宁tellimagrandin II在氧气存在下氧化为二聚体衍生物cornusiin E。这种明显均一的酶制剂的分子量约为160,000(由四个分子量为40,000的亚基组成),最适pH值为5.2,等电点为pH 5.2,在pH 4.3时最稳定。抑制研究表明,这种新酶(建议其系统名称为“tellimagrandin II:O2氧化还原酶”)是酚氧化酶漆酶(EC 1.10.3.2)家族的一员。该酶的性质与一种相关漆酶不同,后者催化1,2,3,4,6 - 五没食子酰葡萄糖向tellimagrandin II的转化,这是cornusiin E生物合成途径中的前一步。