東京大学 · Biochemistry, Genetics and Molecular Biology
이카로 아베 교수의 연구실은 주로 스테롤과 트라이터펜의 생합성에서 핵심적인 역할을 하는 효소, 특히 스쿠알렌 사이클라제와 옥시스쿠알렌 사이클라제의 구조 및 기능을 중심으로 연구를 진행하고 있습니다. 특히 단백질 구조 분석, 유전자 기반 생합성 경로 규명, 그리고 고도로 복잡한 자연물의 구조 결정 기법(예: 결정 스폰지법)을 응용하여 신소재 자연물의 생합성 메커니즘을 밝혀내는 데 초점을 맞추고 있습니다. 최근에는 곰팡이 유래 메로테르펜 및 알로에에서 발견된 신규 타입의 3형 폴리케타이드 합성효소의 기능 규명을 통해 다이버시티가 높은 자연물의 생합성 원리를 탐구하고 있습니다.
표시된 성과는 수집된 데이터 기준으로 산출되며, 일부 차이가 있을 수 있습니다.
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTEnzymatic cyclization of squalene and oxidosqualene to sterols and triterpenesIkuro. Abe, Michel. Rohmer, and Glenn D. PrestwichCite this: Chem. Rev. 1993, 93, 6, 2189–2206Publication Date (Print):September 1, 1993Publication History Published online1 May 2002Published inissue 1 September 1993https://pubs.acs.org/doi/10.1021/cr00022a009https://doi.org/10.1021/cr00022a009research-articleACS PublicationsRequest reuse permissionsArticle Views2803Altmetric
Covering: up to September 2015. Meroterpenoids are hybrid natural products that partially originate from the terpenoid pathway. The meroterpenoids derived from fungi display quite diverse structures, with a wide range of biological properties. This review summarizes the molecular bases for their biosyntheses, which were recently elucidated with modern techniques, and also discusses the plausible biosynthetic pathways of other related natural products lacking genetic information. (Complementary t
Covering: 2002 to 2009
This review covers recent advances in the chemistry and enzymology of squalene cyclase and oxidosqualene cyclase. The enzymatic cyclizations of squalene and oxidosqualene are the most remarkable steps in the biosynthesis of sterols and triterpenes. The polyenes are converted to various polycyclic triterpenes by different enzyme systems employing only small modification of the active-site. Recent crystallographic and structure-based mutagenesis studies as well as utilization of chemically synthes
Genome mining of a terpene synthase gene from Emericella variecolor NBRC 32302 and its functional expression in Aspergillus oryzae led to the production of the new sesterterpene hydrocarbon, astellifadiene (1), having a 6-8-6-5-fused ring system. The structure of 1 was initially investigated by extensive NMR analyses, and was further confirmed by the crystalline sponge method, which established the absolute structure of 1 and demonstrated the usefulness of the method in the structure determinati
The chalcone synthase (CHS) superfamily of type III polyketide synthases (PKSs) produces a variety of plant secondary metabolites with remarkable structural diversity and biological activities (e.g., chalcones, stilbenes, benzophenones, acrydones, phloroglucinols, resorcinols, pyrones, and chromones). Here we describe an octaketide-producing novel plant-specific type III PKS from aloe (Aloe arborescens) sharing 50-60% amino acid sequence identity with other plant CHS-superfamily enzymes. A recom
Di- and sesterterpene synthases produce C20 and C25 isoprenoid scaffolds from geranylgeranyl pyrophosphate (GGPP) and geranylfarnesyl pyrophosphate (GFPP), respectively. By genome mining of the fungus Emericella variecolor, we identified a multitasking chimeric terpene synthase, EvVS, which has terpene cyclase (TC) and prenyltransferase (PT) domains. Heterologous gene expression in Aspergillus oryzae led to the isolation of variediene (1), a novel tricyclic diterpene hydrocarbon. Intriguingly, i
Benzalacetone synthase (BSA) is a novel plant-specific polyketide synthase that catalyzes a one step decarboxylative condensation of 4-coumaroyl-CoA with malonyl-CoA to produce the C6-C4 skeleton of phenylbutanoids in higher plants. A cDNA encoding BAS was for the first time cloned and sequenced from rhubarb (Rheum palmatum), a medicinal plant rich in phenylbutanoids including pharmaceutically important phenylbutanone glucoside, lindleyin. The cDNA encoded a 42-kDa protein that shares 60-75% ami
The first page of this article is displayed as the abstract.
A novel plant-specific type III polyketide synthase (PKS) that catalyzes formation of a pentaketide chromone, 5,7-dihydroxy-2-methylchromone, from five molecules of malonyl-CoA, was cloned and sequenced from aloe (Aloe arborescens). Site-directed mutagenesis revealed that Met207 (corresponding to Thr197 in CHS) determines the polyketide chain length and the product specificity of the enzyme; remarkably, replacement of a single amino acid residue, Met207, with Gly yielded a mutant enzyme that eff
Unexpected methylation: Terretonin is a fungal meroterpenoid derived from 3,5-dimethylorsellinic acid (DMOA). Trt1 is a terpene cyclase involved in terretonin biosynthesis and only accepts the methylated compound as a substrate to produce the cyclized product. Methylation is a common requirement for the cyclization steps in DMOA-derived meroterpenoid biosynthesis. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but n
The products of two bifunctional fungal sesterterpene synthases (StTPS), with prenyl transferase (PT) and terpene synthase (TPS) domains from Penicillium, were structurally characterized and their mechanisms studied in detail by labeling experiments. A phylogenetic analysis of the TPS domains of the new and previously characterized enzymes revealed six distinct clades. Enzymes from the same clade catalyze a common initial cyclization step, which suggests the potential for structural predictions
