106-28-5Relevant articles and documents
Structural and functional analysis of bacillus subtilis yisp reveals a role of its product in biofilm production
Feng, Xinxin,Hu, Yumei,Zheng, Yingying,Zhu, Wei,Li, Kai,Huang, Chun-Hsiang,Ko, Tzu-Ping,Ren, Feifei,Chan, Hsiu-Chien,Nega, Mulugeta,Bogue, Shannon,Lpez, Daniel,Kolter, Roberto,G?tz, Friedrich,Guo, Rey-Ting,Oldfield, Eric
, p. 1557 - 1563 (2014)
YisP is involved in biofilm formation in Bacillus subtilis and has been predicted to produce C30 isoprenoids. We determined the structure of YisP and observed that it adopts the same fold as squalene and dehydrosqualene synthases. However, the first aspartate-rich motif found in essentially all isoprenoid synthases is aspartate poor in YisP and cannot catalyze head-to-head condensation reactions. We find that YisP acts as a phosphatase, catalyzing formation of farnesol from farnesyl diphosphate, and that it is the first phosphatase to adopt the fold seen in the head-to-head prenyl synthases. Farnesol restores biofilm formation in a Δyisp mutant and modifies lipid membrane structure similarly to the virulence factor staphyloxanthin. This work clarifies the role of YisP in biofilm formation and suggests an intriguing possibility that many of the YisP-like homologs found in other bacteria may also have interesting products and functions.
Molecular cloning and characterization of drimenol synthase from valerian plant (Valeriana officinalis)
Kwon, Moonhyuk,Cochrane, Stephen A.,Vederas, John C.,Ro, Dae-Kyun
, p. 4597 - 4603 (2014)
Drimenol, a sesquiterpene alcohol, and its derivatives display diverse bio-activities in nature. However, a drimenol synthase gene has yet to be identified. We identified a new sesquiterpene synthase cDNA (VoTPS3) in valerian plant (Valeriana officinalis). Purification and NMR analyses of the VoTPS3-produced terpene, and characterization of the VoTPS3 enzyme confirmed that VoTPS3 synthesizes (-)-drimenol. In feeding assays, possible reaction intermediates, farnesol and drimenyl diphosphate, could not be converted to drimenol, suggesting that the intermediate remains tightly bound to VoTPS3 during catalysis. A mechanistic consideration of (-)-drimenol synthesis suggests that drimenol synthase is likely to use a protonation-initiated cyclization, which is rare for sesquiterpene synthases. VoTPS3 can be used to produce (-)-drimenol, from which useful drimane-type terpenes can be synthesized.
Roles of rat and human aldo-keto reductases in metabolism of farnesol and geranylgeraniol
Endo, Satoshi,Matsunaga, Toshiyuki,Ohta, Chisato,Soda, Midori,Kanamori, Ayano,Kitade, Yukio,Ohno, Satoshi,Tajima, Kazuo,El-Kabbani, Ossama,Hara, Akira
, p. 261 - 268 (2011)
Farnesol (FOH) and geranylgeraniol (GGOH) with multiple biological actions are produced from the mevalonate pathway, and catabolized into farnesoic acid and geranylgeranoic acid, respectively, via the aldehyde intermediates (farnesal and geranylgeranial). We investigated the intracellular distribution, sequences and properties of the oxidoreductases responsible for the metabolic steps in rat tissues. The oxidation of FOH and GGOH into their aldehyde intermediates were mainly mediated by alcohol dehydrogenases 1 (in the liver and colon) and 7 (in the stomach and lung), and the subsequent step into the carboxylic acids was catalyzed by a microsomal aldehyde dehydrogenase. In addition, high reductase activity catalyzing the aldehyde intermediates into FOH (or GGOH) was detected in the cytosols of the extra-hepatic tissues, where the major reductase was identified as aldo-keto reductase (AKR) 1C15. Human reductases with similar specificity were identified as AKR1B10 and AKR1C3, which most efficiently reduced farnesal and geranylgeranial among seven enzymes in the AKR1A-1C subfamilies. The overall metabolism from FOH to farnesoic acid in cultured cells was significantly decreased by overexpression of AKR1C15, and increased by addition of AKR1C3 inhibitors, tolfenamic acid and R-flurbiprofen. Thus, AKRs (1C15 in rats, and 1B10 and 1C3 in humans) may play an important role in controlling the bioavailability of FOH and GGOH.
Corey,E.J. et al.
, p. 4245 - 4247 (1967)
Substrate specificities of E- and Z-farnesyl diphosphate synthases with substrate analogs
Nagaki, Masahiko,Ichijo, Takumi,Kobashi, Rikiya,Yagihashi, Yusuke,Musashi, Tohru,Kawakami, Jun,Ohya, Norimasa,Gotoh, Takeshi,Sagami, Hiroshi
, p. 1 - 6 (2012)
Prenyltransferases catalyzes the basic isoprenoid chain elongation to produce prenyl diphosphates, which led to upward of 30,000 diverse isoprenoids as steroids, carotenoids, natural rubbers, and prenyl proteins. Here, we determined the reactivities of E- and Z-farnesyl diphosphate synthases (E- and Z-FPP synthases) isolated from Bacillus stearothermophilus and Thermobifida fusca, respectively. For this purpose we use the synthetic substrate analogs, 8-tetrahydropyran-2-yloxy-, 8-hydroxy- and 8-acetoxygeranyl diphosphates. Z-FPP synthase catalyzed the reaction between 8-hydroxygeranyl diphosphate (HOGPP) and isopentenyl diphosphate (IPP), which produced (2Z)-12-hydroxyfarnesyl diphosphate (yield: 16.7%) and (2Z, 6Z)-16-hydroxygeranylgeranyl diphosphate (yield: 6.6%). Neither E- nor Z-farnesyl diphosphate synthases detectably catalyzed reactions between 8-tetrahydropyran-2-yloxygeranyl diphosphate (8-THPOGPP) and IPP. However, a mutated E-FPP synthase (Y81S), did catalyze this reaction, producing 12-tetrahydropyran-2-yloxyfarnesyl diphosphate (12-THPOFPP) with a yield of 12.3%. Wild-type E-FPP synthase catalyzed the reaction of 8-acetoxygeranyl diphosphate (8-AcOGPP) with IPP, which produced 12-acetoxyfarnesyl diphosphate (12-AcOFPP) (yield, 21.8%). Mutant E-FPP synthase catalyzed the reaction between 8-AcOGPP with IPP, producing 12-AcOFPP and 16-acetoxygeranylgeranyl diphosphate (16-AcOGGPP) with respective yields of 55.3% and 1.7%. We believe our results contribute to a better understanding of the catalytic properties of these key enzymes and illustrate their use in the stereo-specific syntheses of compounds that may have significant biotechnological and medical applications.
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Corey,E.J.,Kirst,H.A.
, p. 5041 - 5043 (1968)
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Regiospecific Synthesis of Calcium-Independent Daptomycin Antibiotics using a Chemoenzymatic Method
Mupparapu, Nagaraju,Lin, Yu-Hsin Cindy,Kim, Tae Ho,Elshahawi, Sherif I.
supporting information, p. 4176 - 4182 (2021/02/01)
Daptomycin (DAP) is a calcium (Ca2+)-dependent FDA-approved antibiotic drug for the treatment of Gram-positive infections. It possesses a complex pharmacophore hampering derivatization and/or synthesis of analogues. To mimic the Ca2+-binding effect, we used a chemoenzymatic approach to modify the tryptophan (Trp) residue of DAP and synthesize kinetically characterized and structurally elucidated regiospecific Trp-modified DAP analogues. We demonstrated that the modified DAPs are several times more active than the parent molecule against antibiotic-susceptible and antibiotic-resistant Gram-positive bacteria. Strikingly, and in contrast to the parent molecule, the DAP derivatives do not rely on calcium or any additional elements for activity.
METHOD FOR PRODUCING CARBOXYLIC ACID PRENYL AND PRENOL
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Paragraph 0086-0099, (2019/12/31)
PROBLEM TO BE SOLVED: To provide a method for producing carboxylic acid prenyls and prenols in high yields and in an industrial and economical advantageous manner. SOLUTION: A production method includes reacting a prenyl amine represented by formula (1), in the presence of a halide, with a carboxylic acid anhydride represented by formula (2), to produce a carboxylic acid prenyl represented by formula (3), and further subjecting the carboxylic acid prenyl to solvolysis, to obtain a prenol represented by formula (6). SELECTED DRAWING: None COPYRIGHT: (C)2020,JPOandINPIT
PRODUCTION OF FARNESOL
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Page/Page column 11, (2017/04/11)
The present invention relates to an improved way for the production of farnesol.