Iwaki Hiroaki, Wang Shaozhao, Grosse Stephan, Bergeron Hélène, Nagahashi Ayako, Lertvorachon Jittiwud, Yang Jianzhong, Konishi Yasuo, Hasegawa Yoshie, Lau Peter C K
National Research Council Canada, Biotechnology Research Institute, 6100 Royalmount Avenue, Montreal, Quebec H4P 2R2, Canada.
Appl Environ Microbiol. 2006 Apr;72(4):2707-20. doi: 10.1128/AEM.72.4.2707-2720.2006.
Baeyer-Villiger monooxygenases (BVMOs) are biocatalysts that offer the prospect of high chemo-, regio-, and enantioselectivity in the organic synthesis of lactones or esters from a variety of ketones. In this study, we have cloned, sequenced, and overexpressed in Escherichia coli a new BVMO, cyclopentadecanone monooxygenase (CpdB or CPDMO), originally derived from Pseudomonas sp. strain HI-70. The 601-residue primary structure of CpdB revealed only 29% to 50% sequence identity to those of known BVMOs. A new sequence motif, characterized by a cluster of charged residues, was identified in a subset of BVMO sequences that contain an N-terminal extension of approximately 60 to 147 amino acids. The 64-kDa CPDMO enzyme was purified to apparent homogeneity, providing a specific activity of 3.94 micromol/min/mg protein and a 20% yield. CPDMO is monomeric and NADPH dependent and contains approximately 1 mol flavin adenine dinucleotide per mole of protein. A deletion mutant suggested the importance of the N-terminal 54 amino acids to CPDMO activity. In addition, a Ser261Ala substitution in a Rossmann fold motif resulted in an improved stability and increased affinity of the enzyme towards NADPH compared to the wild-type enzyme (K(m) = 8 microM versus K(m) = 24 microM). Substrate profiling indicated that CPDMO is unusual among known BVMOs in being able to accommodate and oxidize both large and small ring substrates that include C(11) to C(15) ketones, methyl-substituted C(5) and C(6) ketones, and bicyclic ketones, such as decalone and beta-tetralone. CPDMO has the highest affinity (K(m) = 5.8 microM) and the highest catalytic efficiency (k(cat)/K(m) ratio of 7.2 x 10(5) M(-1) s(-1)) toward cyclopentadecanone, hence the Cpd designation. A number of whole-cell biotransformations were carried out, and as a result, CPDMO was found to have an excellent enantioselectivity (E > 200) as well as 99% S-selectivity toward 2-methylcyclohexanone for the production of 7-methyl-2-oxepanone, a potentially valuable chiral building block. Although showing a modest selectivity (E = 5.8), macrolactone formation of 15-hexadecanolide from the kinetic resolution of 2-methylcyclopentadecanone using CPDMO was also demonstrated.
拜耳-维利格单加氧酶(BVMOs)是一类生物催化剂,有望在从各种酮类有机合成内酯或酯的过程中实现高化学选择性、区域选择性和对映选择性。在本研究中,我们从假单胞菌属HI-70菌株中克隆、测序并在大肠杆菌中过表达了一种新的BVMO,环十五烷酮单加氧酶(CpdB或CPDMO)。CpdB的601个氨基酸的一级结构与已知BVMOs的序列同一性仅为29%至50%。在包含约60至147个氨基酸N端延伸的BVMO序列子集中,鉴定出了一个以带电荷残基簇为特征的新序列基序。64 kDa的CPDMO酶被纯化至表观均一,比活性为3.94 μmol/(min·mg蛋白),产率为20%。CPDMO是单体且依赖NADPH,每摩尔蛋白约含1摩尔黄素腺嘌呤二核苷酸。一个缺失突变体表明N端54个氨基酸对CPDMO活性很重要。此外,与野生型酶相比,Rossmann折叠基序中的Ser261Ala取代提高了酶的稳定性,并增加了酶对NADPH的亲和力(K m = 8 μM,而野生型为K m = 24 μM)。底物谱分析表明,CPDMO在已知BVMOs中不同寻常,它能够容纳并氧化大小环底物,包括C(11)至C(15)酮、甲基取代的C(5)和C(6)酮以及双环酮,如十氢萘酮和β-四氢萘酮。CPDMO对环十五烷酮具有最高的亲和力(K m = 5.8 μM)和最高的催化效率(k cat /K m 比值为7.2×10 5 M -1 s -1 ),因此命名为Cpd。进行了一些全细胞生物转化,结果发现CPDMO对2-甲基环己酮具有优异的对映选择性(E > 200)以及99%的S选择性,用于生产7-甲基-2-氧杂环庚酮,这是一种潜在有价值的手性砌块。尽管选择性适中(E = 5.8),但也证明了使用CPDMO从2-甲基环十五烷酮的动力学拆分中形成十五-十六内酯的大环内酯化反应。