Topic
Lanosterol
About: Lanosterol is a research topic. Over the lifetime, 1239 publications have been published within this topic receiving 36737 citations. The topic is also known as: (3β)-lanosta-8,24-dien-3-ol & (3β,20R)-lanosta-8,24-dien-3-ol.
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TL;DR: Investigation of the accumulation of intermediate and by-product and of the expression of three important biosynthetic genes was conducted in liquid shaking and static cultures of G. lucidum to understand the regulation of GA biosynthesis, and higher GA content in liquid static culture was related to increased transcription of those genes especially SQS.
Abstract: Two-stage culture was efficient in enhancing total ganoderic acid (GA) production by Ganoderma lucidum (Fang and Zhong, Biotechnol Prog 18:51-54, 2002). As different GAs have different bioactivities, it is critical to understand the kinetics of individual GA production during fermentation, but no related information is yet available. To understand the regulation of GA biosynthesis, investigation of the accumulation of intermediate (lanosterol) and by-product (ergosterol) and of the expression of three important biosynthetic genes was also conducted in liquid shaking and static cultures of G. lucidum. The results showed that the content of individual GAs increased rapidly in the liquid static culture, and their maximum value was 6- to 25-fold that of shaking culture while lanosterol content in the former was lower than the latter. The transcript of squalene synthase (SQS), lanosterol synthase and 3-hydroxy-3-methylglutaryl coenzyme A reductase in liquid static culture was 4.3-, 2.1-, and 1.9-fold that of the shaking culture, respectively. Higher GA content in liquid static culture was related to increased transcription of those genes especially SQS. The work is helpful to the production of individual GAs and provided an insight into why the liquid static culture was superior to the shaking culture in view of biosynthetic gene expression.
81 citations
TL;DR: The first mammalian cholesterol biosynthetic enzyme unequivocally localized at the surface of intracellular lipid storage droplets is reported, adding to the growing notion that the lipid droplet is an organelle endowed with more complex roles in various biological phenomena.
81 citations
TL;DR: Phenotypes and high-resolution X-ray crystal structures were determined for the mutant enzymes complexing with short-tailed or long-tailed triazoles and wild type enzyme complexed with voriconazole, which appears to be the mechanism by which resistance to these short chain azoles occurs.
Abstract: Emergence of fungal strains showing resistance to triazole drugs can make treatment of fungal disease problematic. Triazole resistance can arise due to single mutations in the drug target lanosterol 14α-demethylase (Erg11p/CYP51). We have determined how commonly occurring single site mutations in pathogenic fungi affect triazole binding using Saccharomyces cerevisiae Erg11p (ScErg11p) as a target surrogate. The mutations Y140F/H were introduced into full-length hexahistidine-tagged ScErg11p. Phenotypes and high-resolution X-ray crystal structures were determined for the mutant enzymes complexed with short-tailed (fluconazole and voriconazole) or long-tailed (itraconazole and posaconazole) triazoles and wild type enzyme complexed with voriconazole. The mutations disrupted a water-mediated hydrogen bond network involved in binding of short-tailed triazoles, which contain a tertiary hydroxyl not present in long-tailed triazoles. This appears to be the mechanism by which resistance to these short chain azoles occurs. Understanding how these mutations affect drug affinity will aid the design of azoles that overcome resistance.
81 citations
TL;DR: A plausible 19-step sequence of enzymatic reactions can now be written as a result of studies that have progressed from organic synthesis of the presumed intermediate, generation of the intermediate in microsomes, further enzyme conversion to cholesterol, Solubilization and purification of the membrane-bound enzyme that acts on the intermediate, and reconstitution of groups of solubilized enzymes into artificial membranes.
80 citations
TL;DR: Comparative DSC and Fourier transform infrared spectroscopic studies indicate that lanosterol is less miscible in DPPC bilayers than is cholesterol, but perturbs their organization to a greater extent, probably due primarily to the rougher faces and larger cross-sectional area of the Lanosterol molecule.
79 citations