Faculty of Pharmaceutical Sciences, Hokkaido University, Kita 12, Nishi 6, Kita-ku, Sapporo 060-0812, Japan.
Global Station for Biosurfaces and Drug Discovery, Hokkaido University, Kita 12, Nishi 6, Sapporo 060-0812, Japan.
J Ind Microbiol Biotechnol. 2021 Jun 4;48(3-4). doi: 10.1093/jimb/kuab023.
Penicillin-binding protein-type thioesterases (PBP-type TEs) are a recently identified group of peptide cyclases that catalyze head-to-tail macrolactamization of nonribosomal peptides. PenA, a new member of this group, is involved in the biosyntheses of cyclic pentapeptides. In this study, we demonstrated the enzymatic activity of PenA in vitro, and analyzed its substrate scope with a series of synthetic substrates. A comparison of the reaction profiles between PenA and SurE, a representative PBP-type TE, showed that PenA is more specialized for small peptide cyclization. A computational model provided a possible structural rationale for the altered specificity for substrate chain lengths.
青霉素结合蛋白型硫酯酶（PBP 型 TE）是最近被鉴定的一类肽环化酶，可催化非核糖体肽的头尾大环内酯化。PenA 是该家族的新成员，参与环状五肽的生物合成。在本研究中，我们在体外证明了 PenA 的酶活性，并使用一系列合成底物分析了其底物范围。PenA 和 SurE（一种代表性的 PBP 型 TE）之间的反应谱比较表明，PenA 更专门用于小肽环化。计算模型为改变的底物链长特异性提供了可能的结构基础。
