Lesburg C A, Lloyd M D, Cane D E, Christianson D W
Department of Chemistry, University of Pennsylvania, Philadelphia 19104, USA.
Protein Sci. 1995 Nov;4(11):2436-8. doi: 10.1002/pro.5560041124.
Recombinant pentalenene synthase, a 42.5-kDa sesquiterpene cyclase originally isolated from Streptomyces UC5319 and cloned in Escherichia coli, has been crystallized in space group P6(3) with unit cell dimensions a = b = 183.5 A and c = 56.5 A. Hexagonal prismatic crystals, approximately 0.2 x 0.2 x 0.3 mm, diffract to approximately 2.9 A resolution using monochromatic synchrotron radiation. From the universal (and achiral) building block, farnesyl pyrophosphate, pentalenene synthase catalyzes the formation of four stereocenters in the construction of the three fused five-membered rings of pentalenene; this novel sesquiterpene is a precursor to the pentalenolactone family of antibiotics.
重组戊烯烯合酶是一种42.5 kDa的倍半萜环化酶，最初从链霉菌UC5319中分离出来并克隆到大肠杆菌中，它已在空间群P6(3)中结晶，晶胞参数a = b = 183.5 Å，c = 56.5 Å。六边形棱柱形晶体，尺寸约为0.2×0.2×0.3 mm，使用单色同步辐射可衍射至约2.9 Å分辨率。从通用（且无手性）的前体法呢基焦磷酸出发，戊烯烯合酶在构建戊烯烯的三个稠合五元环过程中催化形成四个立体中心；这种新型倍半萜是戊烯醇内酯类抗生素的前体。
