Category: 137105-97-6

Ueno, Masaharu; Huang, Yi-Yong; Yamano, Akihito; Kobayashi, Shu published the artcile< Revised Stereochemistry of Ceramide-Trafficking Inhibitor HPA-12 by X-ray Crystallography Analysis>, COA of Formula: C9H15NO4, the main research area is crystal mol structure ceramide trafficking inhibitor HPA; ceramide trafficking inhibitor preparation MSBAR.

In response to Berkes’s report revising the stereochem. of HPA-12, an important ceramide-trafficking inhibitor that was discovered and synthesized and its stereochem. determined in 2001, the synthesis and the stereochem. were reinvestigated. A large-scale synthetic method for HPA-12 based on a Zn-catalyzed asym. Mannich-type reaction in water was developed. Single crystals of HPA-12 for X-ray crystallog. anal. were obtained from Et propionate/n-hexane, and the stereochem. was definitely determined to be 1R,3S, consistent with Berkes’s revised structure.

Organic Letters published new progress about Conformation. 137105-97-6 belongs to class tetrahydrofurans, and the molecular formula is C9H15NO4, COA of Formula: C9H15NO4.

Referemce:
Tetrahydrofuran – Wikipedia,
Tetrahydrofuran | (CH2)3CH2O – PubChem

Ueno, M.; Kitagawa, H.; Ishitani, H.; Yasuda, S.; Hanada, K.; Kobayashi, S. published the artcile< Catalytic enantioselective synthesis of a novel inhibitor of ceramide trafficking, (1R,3R)-N-(3-hydroxy-1-hydroxymethyl-3-phenylpropyl)dodecanamide (HPA-12)>, HPLC of Formula: 137105-97-6, the main research area is HPA12 hydroxyhydroxymethylphenylpropyldodecanamide catalytic enantioselective synthesis ceramide trafficking inhibitor; enantioselective zirconium catalyzed Mannich reaction HPA12 synthesis.

A novel inhibitor of ceramide trafficking, (1R,3R)-N-(3-hydroxy-1-hydroxymethyl-3-phenylpropyl)dodecanamide (HPA-12, I), has been synthesized using a chiral zirconium-catalyzed asym. Mannich-type reaction as a key-step.

Tetrahedron Letters published new progress about Mannich reaction (enantioselective zirconium-catalyzed). 137105-97-6 belongs to class tetrahydrofurans, and the molecular formula is C9H15NO4, HPLC of Formula: 137105-97-6.

Referemce:
Tetrahydrofuran – Wikipedia,
Tetrahydrofuran | (CH2)3CH2O – PubChem

Poudel, Pramod Prasad; Arimitsu, Kenji; Yamamoto, Kana published the artcile< Self-assembled ion-pair organocatalysis - asymmetric Baeyer-Villiger oxidation mediated by flavinium-cinchona alkaloid dimer>, Recommanded Product: (R)-tert-Butyl (5-oxotetrahydrofuran-3-yl)carbamate, the main research area is flavinium cinchona alkaloid dimer organocatalysis asym Baeyer Villiger oxidation.

An ion-pair catalyst generated by assembly of a chiral flavinium and a cinchona alkaloid dimer for use in asym. Baeyer-Villiger oxidation is presented. Ion-pair formation is essential for enhancing the catalytic activity and stereoselectivity. The catalyst is applicable to structurally diverse 3-substituted cyclobutanones, providing good to excellent enantioselectivities (up to 98 : 2 e.r.). This study provides the first example of self-assembly of a flavin derivative and a base to form a chiral reaction site that enables a highly stereoselective reaction to occur.

Chemical Communications (Cambridge, United Kingdom) published new progress about Baeyer-Villiger oxidation. 137105-97-6 belongs to class tetrahydrofurans, and the molecular formula is C9H15NO4, Recommanded Product: (R)-tert-Butyl (5-oxotetrahydrofuran-3-yl)carbamate.

Referemce:
Tetrahydrofuran – Wikipedia,
Tetrahydrofuran | (CH2)3CH2O – PubChem

Chung, Sang J.; Chung, Suhman; Lee, Hyun Soo; Kim, Eun-Jung; Oh, Kyung Seok; Choi, Hyuk Soon; Kim, Kwang S.; Kim, Yeoun Jin; Hahn, Jong Hoon; Kim, Dong H. published the artcile< Mechanistic Insight into the Inactivation of Carboxypeptidase A by α-Benzyl-2-oxo-1,3-oxazolidine-4-acetic Acid, a Novel Type of Irreversible Inhibitor for Carboxypeptidase A with No Stereospecificity>, Category: tetrahydrofurans, the main research area is carboxypeptidase A inactivation oxazolidine derivative.

On the basis of the active site topol. and enzymic catalytic mechanism of carboxypeptidase A (CPA), a prototypical zinc-containing proteolytic enzyme, α-benzyl-2-oxo-1,3-oxazolidine-4-acetic acid (1), was designed as a novel type of mechanism-based inactivator of the enzyme. All four possible stereoisomers of the inhibitor were synthesized in an enantiomerically pure form starting with optically active aspartic acid, and their CPA inhibitory activities were evaluated to find that surprisingly all of the four stereoisomers inhibit CPA in a time dependent manner. The inhibited enzyme did not regain its enzymic activity upon dialysis. The inactivations were prevented by 2-benzylsuccinic acid, a competitive inhibitor that is known to bind the active site of the enzyme. These kinetic results strongly support that the inactivators attach covalently to the enzyme at the active site. The anal. of ESI mass spectral data of the inactivated CPA ascertained the conclusion from the kinetic results. The values of second-order inhibitory rate constants (kobs/[I]o) fall in the range of 1.7-3.6 M-1 min-1. The lack of stereospecificity shown in the inactivation led us to propose that the ring cleavage occurs by the nucleophilic attack at the 2-position rather than at the 5-position and the ring opening takes place in an addition-elimination mechanism. The tetrahedral transition state that would be generated in this pathway is thought to be stabilized by the active site zinc ion, which was supported by the PM3 semiempirical calculations In addition, α-benzyl-2-oxo-1,3-oxazolidine-5-acetic acid (18), a structural isomer of 1 was also found to inactivate CPA in an irreversible manner, reinforcing the nucleophilic addition-elimination mechanism. The present study demonstrates that the transition state for the inactivation pathway plays a critical role in determining stereochem. of the inactivation.

Journal of Organic Chemistry published new progress about Enzyme inhibition kinetics. 137105-97-6 belongs to class tetrahydrofurans, and the molecular formula is C9H15NO4, Category: tetrahydrofurans.

Referemce:
Tetrahydrofuran – Wikipedia,
Tetrahydrofuran | (CH2)3CH2O – PubChem

Bergman, Ylva; Ciampini, Marisa; Jalal, Sania; Lagiakos, Helen Rachel; Aguilar, Marie-Isabel; Perlmutter, Patrick published the artcile< The synthesis of Fmoc-O-allyl β-serine>, Related Products of 137105-97-6, the main research area is serine beta allyl Fmoc protected synthesis diazomethane safety; allyl serine Boc protected Arndt Eistert homologation Seebach safety; aspartic acid tertbutoxycarbonyl protected allylation.

Two concise routes for the synthesis of the title amino acid have been developed. The first route employs Seebach’s general approach with Arndt Eistert homologation of Boc-O-allyl α-serine (Boc = tert-butoxycarbonyl) as the key process. The second route employs an approach using Boc-α-aspartic acid as a starting material with a selective palladium-catalyzed O-allylation as key processes. These two routes are evaluated for their relative efficiency and safety.

Tetrahedron: Asymmetry published new progress about Allylation. 137105-97-6 belongs to class tetrahydrofurans, and the molecular formula is C9H15NO4, Related Products of 137105-97-6.

Referemce:
Tetrahydrofuran – Wikipedia,
Tetrahydrofuran | (CH2)3CH2O – PubChem

Chung, Sang J.; Chung, Suhman; Lee, Hyun Soo; Kim, Eun-Jung; Oh, Kyung Seok; Choi, Hyuk Soon; Kim, Kwang S.; Kim, Yeoun Jin; Hahn, Jong Hoon; Kim, Dong H. published the artcile< Mechanistic Insight into the Inactivation of Carboxypeptidase A by α-Benzyl-2-oxo-1,3-oxazolidine-4-acetic Acid, a Novel Type of Irreversible Inhibitor for Carboxypeptidase A with No Stereospecificity>, Product Details of C9H15NO4, the main research area is carboxypeptidase A inactivation oxazolidine derivative.

On the basis of the active site topol. and enzymic catalytic mechanism of carboxypeptidase A (CPA), a prototypical zinc-containing proteolytic enzyme, α-benzyl-2-oxo-1,3-oxazolidine-4-acetic acid (1), was designed as a novel type of mechanism-based inactivator of the enzyme. All four possible stereoisomers of the inhibitor were synthesized in an enantiomerically pure form starting with optically active aspartic acid, and their CPA inhibitory activities were evaluated to find that surprisingly all of the four stereoisomers inhibit CPA in a time dependent manner. The inhibited enzyme did not regain its enzymic activity upon dialysis. The inactivations were prevented by 2-benzylsuccinic acid, a competitive inhibitor that is known to bind the active site of the enzyme. These kinetic results strongly support that the inactivators attach covalently to the enzyme at the active site. The anal. of ESI mass spectral data of the inactivated CPA ascertained the conclusion from the kinetic results. The values of second-order inhibitory rate constants (kobs/[I]o) fall in the range of 1.7-3.6 M-1 min-1. The lack of stereospecificity shown in the inactivation led us to propose that the ring cleavage occurs by the nucleophilic attack at the 2-position rather than at the 5-position and the ring opening takes place in an addition-elimination mechanism. The tetrahedral transition state that would be generated in this pathway is thought to be stabilized by the active site zinc ion, which was supported by the PM3 semiempirical calculations In addition, α-benzyl-2-oxo-1,3-oxazolidine-5-acetic acid (18), a structural isomer of 1 was also found to inactivate CPA in an irreversible manner, reinforcing the nucleophilic addition-elimination mechanism. The present study demonstrates that the transition state for the inactivation pathway plays a critical role in determining stereochem. of the inactivation.

Journal of Organic Chemistrypublished new progress about Enzyme inhibition kinetics. 137105-97-6 belongs to class tetrahydrofurans, and the molecular formula is C9H15NO4, Product Details of C9H15NO4.

Referemce:
Tetrahydrofuran – Wikipedia,
Tetrahydrofuran | (CH2)3CH2O – PubChem