Burmester J, Haese A, Zocher R
Institut für Biochemie und Molekulare Biologie, Technische Universität Berlin, Federal Republic of Germany.
Biochem Mol Biol Int. 1995 Oct;37(2):201-7.
The methyltransferase portion of the N-methyl-peptide-synthetase gene, synthesizing enniatin from Fusarium sambucinum, was amplified with the polymerase chain reaction (PCR) using primers derived from the highly conserved sequences of the flanking peptide synthetase domain. The deduced amino acid sequence of the product shares high similarity to the 430 amino acid methyltransferase portion of enniatin synthetase of Fusarium scirpi and the corresponding portions of another fungal peptide synthetase catalyzing the biosynthesis of the N-methylated cyclopeptide cyclosporin. As the methyltransferase portions show only local similarity to motifs apparently conserved within methyltransferases, the segments of peptide synthetases involved in the biosynthesis of bioactive peptides represent a new class of S-adenosyl-L-methionine dependent methyltransferases.
利用聚合酶链反应（PCR），使用从侧翼肽合成酶结构域的高度保守序列衍生而来的引物，扩增了来自拟分枝镰刀菌的N-甲基肽合成酶基因的甲基转移酶部分，该部分负责从拟分枝镰刀菌合成恩镰孢菌素。所推导的产物氨基酸序列与尖孢镰刀菌恩镰孢菌素合成酶的430个氨基酸甲基转移酶部分以及另一种催化N-甲基化环肽环孢菌素生物合成的真菌肽合成酶的相应部分具有高度相似性。由于甲基转移酶部分仅与甲基转移酶内明显保守的基序表现出局部相似性，参与生物活性肽生物合成的肽合成酶片段代表了一类新的依赖S-腺苷-L-甲硫氨酸的甲基转移酶。
