327175-05-3

Usage

Uses

Used in Pharmaceutical Industry:
2H-Pyran-2-one, 4-hydroxy-6-(2-oxoheptyl)is used as a pharmaceutical compound for its potential therapeutic applications. 2H-Pyran-2-one, 4-hydroxy-6-(2-oxoheptyl)-'s unique structure and properties may allow it to interact with specific biological targets, making it a promising candidate for the development of new drugs. Its production through Mycobacterium tuberculosis, a well-studied bacterium, may also provide insights into its potential uses in treating tuberculosis or other related diseases.
Used in Chemical Research:
In the field of chemical research, 2H-Pyran-2-one, 4-hydroxy-6-(2-oxoheptyl)can be used as a starting material or intermediate for the synthesis of more complex molecules. Its unique structure may enable the development of novel chemical reactions or the creation of new compounds with specific properties and applications.
Used in Material Science:
2H-Pyran-2-one, 4-hydroxy-6-(2-oxoheptyl)-'s structural characteristics may also make it a candidate for use in material science, where it could be employed in the development of new materials with specific properties. For example, its potential to form stable complexes with other molecules could be utilized in the creation of advanced materials with applications in various industries, such as electronics, energy, or environmental protection.
Used in Drug Delivery Systems:
Similar to gallotannin, 2H-Pyran-2-one, 4-hydroxy-6-(2-oxoheptyl)could be used in drug delivery systems to improve the bioavailability and therapeutic outcomes of various drugs. Its unique structure may allow for the development of novel drug carriers or the enhancement of existing drug delivery methods, leading to more effective treatments for a range of diseases.

Upstream product

• 524-14-1 malonyl-CoA 
• 21708-76-9 hexanoyl-CoA 
• 524-14-1 S-(hydrogen malonyl)coenzyme A 
• 5060-32-2 S-hexanoyl-coenzyme-A 
• 21708-76-9 hexanoyl-CoA ester 

Relevant academic research and scientific papers

Cloning and structure-function analyses of quinolone- and acridone-producing novel type III polyketide synthases from citrus microcarpa

Background:Type III polyketide synthases (PKSs) synthesize various polyketide and alkaloid scaffolds. Results:QNS synthesizes quinolone as the single product, whereas ACS produces acridone as the major product. Conclusion:QNS and ACS are novel quinolone- and acridone-producing type III PKSs, respectively. Significance:Structure-function analyses of QNS and ACS provide insights into molecular bases for alkaloid biosyntheses.

Alkylresorcylic acid synthesis by type III polyketide synthases from rice Oryza sativa

Alkylresorcinols, produced by various plants, bacteria, and fungi, are bioactive compounds possessing beneficial activities for human health, such as anti-cancer activity. In rice, they accumulate in seedlings, contributing to protection against fungi. Alkylresorcylic acids, which are carboxylated forms of alkylresorcinols, are unstable compounds and decarboxylate readily to yield alkylresorcinols. Genome mining of the rice Oryza sativa identified two type III polyketide synthases, named ARAS1 (alkylresorcylic acid synthase) and ARAS2, that catalyze the formation of alkylresorcylic acids. Both enzymes condensed fatty acyl-CoAs with three C2 units from malonyl-CoA and cyclized the resulting tetraketide intermediates via intramolecular C-2 to C-7 aldol condensation. The alkylresorcylic acids thus produced were released from the enzyme and decarboxylated non-enzymatically to yield alkylresorcinols. This is the first report on a plant type III polyketide synthase that produces tetraketide alkylresorcylic acids as major products.

In vitro precursor-directed synthesis of polyketide analogues with coenzyme a regeneration for the development of antiangiogenic agents

Polyketide analogues are produced via in vitro reconstruction of a precursor-directed polyketide biosynthetic pathway. Malonyl-CoA synthetase (MCS) was used in conjunction with chalcone synthase (CHS), thereby allowing efficient use of synthetic starter molecules and malonate as extender. Coenzyme-A was recycled up to 50 times. The use of a simple immobilization procedure resulted in up to a 30-fold higher yield of pyrone CHS products than that obtained with the free enzyme solutions.

Pyrone polyketides synthesized by a type III polyketide synthase from Drosophyllum lusitanicum

To isolate cDNAs involved in the biosynthesis of acetate-derived naphthoquinones in Drosophyllum lusitanicum, an expressed sequence tag analysis was performed. RNA from callus cultures was used to create a cDNA library from which 2004 expressed sequence tags were generated. One cDNA with similarity to known type III polyketide synthases was isolated as full-length sequence and termed DluHKS. The translated polypeptide sequence of DluHKS showed 51-67% identity with other plant type III PKSs. Recombinant DluHKS expressed in Escherichia coli accepted acetyl-coenzyme A (CoA) as starter and carried out sequential decarboxylative condensations with malonyl-CoA yielding α-pyrones from three to six acetate units. However, naphthalenes, the expected products, were not isolated. Since the main compound produced by DluHKS is a hexaketide α-pyrone, and the naphthoquinones in D. lusitanicum are composed of six acetate units, we propose that the enzyme provides the backbone of these secondary metabolites. An involvement of accessory proteins in this biosynthetic pathway is discussed.

Exploiting the reaction flexibility of a type III polyketide synthase through in vitro pathway manipulation

A synthetic metabolic pathway has been constructed in vitro consisting of the type III polyketide synthase from Streptomyces coelicolor and peroxidases from soybean and Caldariomyces fumago (chloroperoxidase). This has resulted in the synthesis of the pentaketide flaviolin and its dimeric derivative, and a wide range of pyrones and their coupled derivatives with flaviolin, as well as their halogenated derivatives. The addition of acyl-CoA oxidase to the pathway prior to the polyketide synthase resulted in unsaturated pyrone side chains, further broadening the product spectrum that can be achieved. The approach developed in this work, therefore, provides a new model to exploit biocatalysis in the synthesis of complex natural product derivatives. Copyright

Enzymatic formation of long-chain polyketide pyrones by plant type III polyketide synthases

Recombinant chalcone synthase from Scutellaria baicalensis and stilbene synthase from Arachis hypogaea accepted CoA esters of long-chain fatty acid as a starter substrate, and carried out sequential condensations with malonyl-CoA, leading to formation of triketide and tetraketide α-pyrones. Recombinant chalcone synthase (CHS) from Scutellaria baicalensis and stilbene synthase (STS) from Arachis hypogaea accepted CoA esters of long-chain fatty acid (CHS up to the C12 ester, while STS up to the C14 ester) as a starter substrate, and carried out sequential condensations with malonyl-CoA, leading to formation of triketide and tetraketide α-pyrones. Interestingly, the C6, C8, and C10 esters were kinetically favored by the enzymes over the physiological starter substrate; the k cat/KM values were 1.2- to 1.9-fold higher than that of p-coumaroyl-CoA. The catalytic diversities of the enzymes provided further mechanistic insights into the type III PKS reactions, and suggested involvement of the CHS-superfamily enzymes in the biosynthesis of long-chain alkyl polyphenols such as urushiol and ginkgolic acid in plants.