Haese A, Schubert M, Herrmann M, Zocher R
Institut für Biochemie und Molekulare Biologie, Technische Universität Berlin, Germany.
Mol Microbiol. 1993 Mar;7(6):905-14. doi: 10.1111/j.1365-2958.1993.tb01181.x.
The gene encoding the multifunctional enzyme enniatin synthetase from Fusarium scirpi (esyn1) was isolated and characterized by transcriptional mapping and expression studies in Escherichia coli. This is the first example of a gene encoding an N-methyl peptide synthetase. The nucleotide sequence revealed an open reading frame of 9393 bp encoding a protein of 3131 amino acids (M(r) 346,900). Two domains designated EA and EB within the protein were identified which share similarity to each other and to microbial peptide synthetase domains. In contrast to the N-terminal domain EA, the carboxyl terminal domain EB is interrupted by a 434-amino-acid portion which shows local similarity to a motif apparently conserved within adenine and cytosine RNA and DNA methyltransferases and therefore seems to harbour the N-methyl-transferase function of the multienzyme.
通过转录图谱分析和在大肠杆菌中的表达研究，分离并鉴定了来自尖孢镰刀菌（Fusarium scirpi）的编码多功能酶恩镰孢菌素合成酶（esyn1）的基因。这是编码N-甲基肽合成酶的基因的首个实例。核苷酸序列显示一个9393 bp的开放阅读框，编码一个由3131个氨基酸组成的蛋白质（M(r) 346,900）。在该蛋白质中鉴定出两个分别命名为EA和EB的结构域，它们彼此相似，且与微生物肽合成酶结构域相似。与N端结构域EA不同，羧基端结构域EB被一个434个氨基酸的部分中断，该部分与腺嘌呤和胞嘧啶RNA及DNA甲基转移酶中一个明显保守的基序具有局部相似性，因此似乎具有该多酶的N-甲基转移酶功能。
