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(+)-(1S,5R)-3-oxabicyclo<3.3.0>oct-6-en-2-one is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

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  • 103618-27-5 Structure
  • Basic information

    1. Product Name: (+)-(1S,5R)-3-oxabicyclo<3.3.0>oct-6-en-2-one
    2. Synonyms: (+)-(1S,5R)-3-oxabicyclo<3.3.0>oct-6-en-2-one
    3. CAS NO:103618-27-5
    4. Molecular Formula:
    5. Molecular Weight: 124.139
    6. EINECS: N/A
    7. Product Categories: N/A
    8. Mol File: 103618-27-5.mol
  • Chemical Properties

    1. Melting Point: N/A
    2. Boiling Point: N/A
    3. Flash Point: N/A
    4. Appearance: N/A
    5. Density: N/A
    6. Refractive Index: N/A
    7. Storage Temp.: N/A
    8. Solubility: N/A
    9. CAS DataBase Reference: (+)-(1S,5R)-3-oxabicyclo<3.3.0>oct-6-en-2-one(CAS DataBase Reference)
    10. NIST Chemistry Reference: (+)-(1S,5R)-3-oxabicyclo<3.3.0>oct-6-en-2-one(103618-27-5)
    11. EPA Substance Registry System: (+)-(1S,5R)-3-oxabicyclo<3.3.0>oct-6-en-2-one(103618-27-5)
  • Safety Data

    1. Hazard Codes: N/A
    2. Statements: N/A
    3. Safety Statements: N/A
    4. WGK Germany:
    5. RTECS:
    6. HazardClass: N/A
    7. PackingGroup: N/A
    8. Hazardous Substances Data: 103618-27-5(Hazardous Substances Data)

103618-27-5 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 103618-27-5 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,0,3,6,1 and 8 respectively; the second part has 2 digits, 2 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 103618-27:
(8*1)+(7*0)+(6*3)+(5*6)+(4*1)+(3*8)+(2*2)+(1*7)=95
95 % 10 = 5
So 103618-27-5 is a valid CAS Registry Number.

103618-27-5SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 12, 2017

Revision Date: Aug 12, 2017

1.Identification

1.1 GHS Product identifier

Product name (+)-(1S,5R)-3-oxabicyclo[3.3.0]oct-6-en-2-one

1.2 Other means of identification

Product number -
Other names (1S,5R)-3-oxabicyclo[3.3.0]oct-6-en-2-one

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:103618-27-5 SDS

103618-27-5Relevant articles and documents

Synthesis of (+/-)-Desmarestene and (+/-)-Viridiene, the Two Sperm Releasing and Attracting Pheromones from the Brown Algae Desmarestia aculeata and Desmarestia viridis

Boland, Wilhelm,Jakoby, Karin,Jaenicke, Lothar

, p. 2355 - 2362 (1982)

Desmarestene 1 6-(1Z,3-butadienyl)-1,4-cycloheptadiene) and viridiene 3 cis-3-(1Z,3-butadienyl)-4-vinylcyclopentene) are chemical messengers for male gametes of the brown algae Desmarestia aculeata and Desmarestia viridis.Total syntheses of 1, 3 and their stereoisomers 1a, 3a-c are reported.Gas-chromatographic comparison of synthetic 1 and 3 with the corresponding natural products has established their structural identity.

Characterization and Crystal Structure of a Robust Cyclohexanone Monooxygenase

Romero, Elvira,Castellanos, J. Rubén Gómez,Mattevi, Andrea,Fraaije, Marco W.

, p. 15852 - 15855 (2016)

Cyclohexanone monooxygenase (CHMO) is a promising biocatalyst for industrial reactions owing to its broad substrate spectrum and excellent regio-, chemo-, and enantioselectivity. However, the low stability of many Baeyer–Villiger monooxygenases is an obstacle for their exploitation in industry. Characterization and crystal structure determination of a robust CHMO from Thermocrispum municipale is reported. The enzyme efficiently converts a variety of aliphatic, aromatic, and cyclic ketones, as well as prochiral sulfides. A compact substrate-binding cavity explains its preference for small rather than bulky substrates. Small-scale conversions with either purified enzyme or whole cells demonstrated the remarkable properties of this newly discovered CHMO. The exceptional solvent tolerance and thermostability make the enzyme very attractive for biotechnology.

Resolution of fused bicyclic ketones by a recombinant biocatalyst expressing the Baeyer-Villiger monooxygenase gene Rv3049c from Mycobacterium tuberculosis H37Rv

Snajdrova, Radka,Grogan, Gideon,Mihovilovic, Marko D.

, p. 4813 - 4817 (2006)

Recombinant Escherichia coli B834 (DE3) pDB5 expressing the Rv3049c gene encoding a Baeyer-Villiger monooxygenase from Mycobacterium tuberculosis H37Rv was used for regioselective oxidations of fused bicyclic ketones. This whole-cell system represents the first recombinant Baeyer-Villiger oxidation biocatalyst that effectively resolves the racemic starting materials in this series. Within biotransformations using this organism one substrate enantiomer remains in high optical purity, while the second enantiomer is oxidized to one type of regioisomeric lactone preferably.

Stereochemical congruence of Baeyer-Villigerases

Kelly, David R.,Knowles, Christopher J.,Mahdi, Jassem G.,Wright, Michael A.,Taylor, Ian N.,Roberts, Stanley M.,Wan, Peter W. H.,Grogan, Gideon,Pedragosa-Moreau, Sandrine,Willetts, Andrew J.

, p. 2333 - 2334 (1996)

The enantiomeric bicyclic ketones 1, 3 and the tricyclic ketone 5 undergo stereochemically congruent Baeyer-Villiger oxidations with CHMO from Acinetobacter sp., CPMO from Pseudomonas sp. as well as 2,5-DKCMO, 3,6-DKCMO and MO2 from P. putida; in every case the tricyclic ketone 5 is transformed with > 96% ee. N-terminal sequences for the FAD/NADPH linked enzymes from Acinetobacter sp., Pseudomonas sp. and a novel CHMO from R. coprophilus have high homology with each other but no homology with the FMN/NADH linked enzymes; 2,5-DKCMO and 3,6-DKCMO.

Divorce in the two-component BVMO family: The single oxygenase for enantioselective chemo-enzymatic Baeyer-Villiger oxidations

R?llig, Robert,Paul, Caroline E.,Claeys-Bruno, Magalie,Duquesne, Katia,Kara, Selin,Alphand, Véronique

, p. 3441 - 3450 (2021)

Two-component flavoprotein monooxygenases consist of a reductase and an oxygenase enzyme. The proof of functionality of the latter without its counterpart as well as the mechanism of flavin transfer remains unanswered beyond doubt. To tackle this question, we utilized a reductase-free reaction system applying purified 2,5-diketocamphane-monooxygenase I (2,5-DKCMO), a FMN-dependent type II Baeyer-Villiger monooxygenase, and synthetic nicotinamide analogues (NCBs) as dihydropyridine derivatives for FMN reduction. This system demonstrated the stand-alone quality of the oxygenase, as well as the mechanism of FMNH2transport by free diffusion. The efficiency of this reductase-free system strongly relies on the balance of FMN reduction and enzymatic (re)oxidation, since reduced FMN in solution causes undesired side reactions, such as hydrogen peroxide formation. Design of experiments allowed us to (i) investigate the effect of various reaction parameters, underlining the importance to balance the FMN/FMNH2cycle, (ii) optimize the reaction system for the enzymatic Baeyer-Villiger oxidation of rac-bicyclo[3.2.0]hept-2-en-6-one,rac-camphor, andrac-norcamphor. Finally, this study not only demonstrates the reductase-independence of 2,5-DKCMO, but also revisits the terminology of two-component flavoprotein monooxygenases for this specific case.

A Flavoprotein Monooxygenase that Catalyses a Baeyer-Villiger Reaction and Thioether Oxidation Using NADH as the Nicotinamide Cofactor

Jensen, Chantel N.,Cartwright, Jared,Ward, Jonathan,Hart, Sam,Turkenburg, Johan P.,Ali, Sohail T.,Allen, Michael J.,Grogan, Gideon

, p. 872 - 878 (2012)

A gene from the marine bacterium Stenotrophomonas maltophilia encodes a 38.6 kDa FAD-containing flavoprotein (Uniprot B2FLR2) named S. maltophilia flavin-containing monooxygenase (SMFMO), which catalyses the oxidation of thioethers and also the regioselective Baeyer-Villiger oxidation of the model substrate bicyclo[3.2.0]hept-2-en-6-one. The enzyme was unusual in its ability to employ either NADH or NADPH as nicotinamide cofactor. The KM and kcat values for NADH were 23.7±9.1 μM and 0.029 s-1 and 27.3±5.3 μM and 0.022 s-1 for NADPH. However, kcat/KM value for the ketone substrate in the presence of 100 μM cofactor was 17 times greater for NADH than for NADPH. SMFMO catalysed the quantitative conversion of 5 mM ketone in the presence of substoichiometric concentrations of NADH with the formate dehydrogenase cofactor recycling system, to give the 2-oxa and 3-oxa lactone products of Baeyer-Villiger reaction in a ratio of 5:1, albeit with poor enantioselectivity. The conversion with NADPH was 15%. SMFMO also catalysed the NADH-dependent transformation of prochiral aromatic thioethers, giving in the best case, 80% ee for the transformation of p-chlorophenyl methyl sulfide to its R enantiomer. The structure of SMFMO reveals that the relaxation in cofactor specificity appears to be accomplished by the substitution of an arginine residue, responsible for recognition of the 2′-phosphate on the NADPH ribose in related NADPH-dependent FMOs, with a glutamine residue in SMFMO. SMFMO is thus representative of a separate class of single-component, flavoprotein monooxygenases that catalyse NADH-dependent oxidations from which possible sequences and strategies for developing NADH-dependent biocatalysts for asymmetric oxygenation reactions might be identified.

Discovery of Baeyer-Villiger monooxygenases from photosynthetic eukaryotes

Beneventi, Elisa,Niero, Mattia,Motterle, Riccardo,Fraaije, Marco,Bergantino, Elisabetta

, p. 145 - 154 (2013)

Baeyer-Villiger monooxygenases are attractive "green" catalysts able to produce chiral esters or lactones starting from ketones. They can act as natural equivalents of peroxyacids that are the catalysts classically used in the organic synthesis reactions, consisting in the cleavage of CC bonds with the concomitant insertion of an oxygen atom. In this study, two type I BVMOs have been identified for the first time in photosynthetic eukaryotic organisms, the red alga Cyanidioschyzon merolae (Cm) and the moss Physcomitrella patens (Pp). A biocatalytic characterization of these newly discovered enzymes, expressed in recombinant forms, was carried out. Both enzymes could be purified as holo enzymes containing a FAD cofactor. Their thermostability was investigated and revealed that the Cm-BVMO is the most thermostable type I BVMO with an apparent melting temperature of 56 C. Substrate profiling revealed that both eukaryotic BVMOs accept a wide range of ketones which include aromatic, aliphatic, aryl aliphatic and bicyclic ketones. In particular, linear aliphatic ketones (C9 and C12), carrying the keto functionality in different positions, resulted to be the best substrates in steady state kinetic analyses. In order to restore the BVMO-typifying sequence motif in the Pp-BVMO, a mutant was prepared (Y160H). Intriguingly, this mutation resulted in higher activities on most tested substrates. The recombinant enzymes displayed kcat values in the 0.1-0.2 s-1 range, which is relatively low when compared with other known type I BVMOs. This may hint to a role in secondary metabolism in these photosynthetic organisms, though their exact function remains to be established.

Intramolecular Cyclopentene Annulation. 3. Synthesis and Carbon-13 Nuclear Magnetic Resonance Spectroscopy of Bicyclic Cyclopentene Lactones as Potential Perhydroazulene and/or Monoterpene Synthons

Hudlicky, Tomas,Reddy, D. Bhaskar,Govindan, S. V.,Kulp, Thomas,Still, Bobbi,Sheth, Jagdish P.

, p. 3422 - 3428 (1983)

The internal cyclopropanation of several diversely substituted dienic diazo esters is described.Thermolysis of the resulting vinylcyclopropanes yielded cyclopentene-annulated lactones in good yields.Depending on the choice of the dienyl unit, either guaiane or pseudoguaiane substitution patterns of the cyclopentene portion were obtained.Stereochemical assignments based on 13C NMR data are provided for all of these lactones.Subsequent transformations of the bicyclic lactones to differentially functionalized cyclopentenes are described.The potential of these synthons in the synthesis of perhydroazulene sesquiterpenes and several monoterpene cyclopentanoid natural products is addressed.

Controlling the Regioselectivity of Baeyer–Villiger Monooxygenases by Mutation of Active-Site Residues

Balke, Kathleen,B?umgen, Marcus,Bornscheuer, Uwe T.

, p. 1627 - 1638 (2017)

Baeyer–Villiger monooxygenase (BVMO)-mediated regiodivergent conversions of asymmetric ketones can lead to the formation of “normal” or “abnormal” lactones. In a previous study, we were able to change the regioselectivity of a BVMO by mutation of the active-site residues to smaller amino acids, which thus created more space. In this study, we demonstrate that this method can also be used for other BVMO/substrate combinations. We investigated the regioselectivity of 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase from Pseudomonas putida (OTEMO) for cis-bicyclo[3.2.0]hept-2-en-6-one (1) and trans-dihydrocarvone (2), and we were able to switch the regioselectivity of this enzyme for one of the substrate enantiomers. The OTEMO wild-type enzyme converted (?)-1 into an equal (50:50) mixture of the normal and abnormal products. The F255A/F443V variant produced 90 % of the normal product, whereas the W501V variant formed up to 98 % of the abnormal product. OTEMO F255A exclusively produced the normal lactone from (+)-2, whereas the wild-type enzyme was selective for the production of the abnormal product. The positions of these amino acids were equivalent to those mutated in the cyclohexanone monooxygenases from Arthrobacter sp. and Acinetobacter sp. (CHMOArthro and CHMOAcineto) to switch their regioselectivity towards (+)-2, which suggests that there are hot spots in the active site of BVMOs that can be targeted with the aim to change the regioselectivity.

Genome mining reveals new bacterial type I Baeyer-Villiger monooxygenases with (bio)synthetic potential

Bianchi, Dario A.,Carabajal, María Ayelén,Ceccoli, Romina D.,Rial, Daniela V.

, (2020)

Baeyer-Villiger monooxygenases (BVMOs) are oxidorreductases that catalyze the oxidation of ketones in a very selective manner. By genome mining we detected seven putative type I BVMOs in Bradyrhizobium diazoefficiens USDA 110. As we established the phylogenetic relationships among them and with other type I BVMOs, we found out that they belong to different clades of the phylogenetic tree. Thus, we decided to clone and heterologously express five of them. Three of them, each one from a divergent phylogenetic group, were obtained as soluble proteins, allowing us to proceed with their biocatalytic assessment and enzymatic characterization. As to substrate scope and selectivity, we observed a complementary behavior among the three BVMOs. BVMO2 was the more versatile biocatalyst in whole-cell systems while BVMO4 and BVMO5 showed a narrow substrate profile with preference for linear ketones and particular regioselectivity for (±)-cis-bicyclo[3.2.0]hept-2-en-6-one.

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