Kakudo S, Negoro S, Urabe I, Okada H
Department of Biotechnology, Osaka University, Japan.
Appl Environ Microbiol. 1993 Nov;59(11):3978-80. doi: 10.1128/aem.59.11.3978-3980.1993.
A new type of nylon oligomer degradation enzyme (EIII) was purified from an Escherichia coli clone harboring the EIII gene (nylC). This enzyme hydrolyzed the linear trimer, tetramer, and pentamer of 6-aminohexanoate by an endo-type reaction, and this specificity is different from that of the EI (nylA gene product) and EII (nylB gene product). Amino acid sequencing and sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified EIII demonstrated that the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267.
从携带EIII基因（nylC）的大肠杆菌克隆中纯化出一种新型尼龙低聚物降解酶（EIII）。该酶通过内切型反应水解6-氨基己酸的线性三聚体、四聚体和五聚体，这种特异性不同于EI（nylA基因产物）和EII（nylB基因产物）。纯化后的EIII的氨基酸测序和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳表明，该酶由两条多肽链组成，这两条链源于氨基酸残基266和267之间的内部切割。
