133192-43-5

Upstream product

• 17150-62-8 N-benzyl-3-butenylamine 
• 298-12-4 Glyoxilic acid 
• 100-46-9 benzylamine 
• 88381-98-0 N-(1-phenyl-3-butenyl)benzylamine 

Downstream Products

• 133192-44-6 methyl cis-4-hydroxy-2-piperidinecarboxylate 
• 1844-40-2 (2S,4R)-4-hydroxypiperidine-2-carboxylic acid 
• 133192-47-9 bis(phenylmethyl) cis-4-(diphenylphosphonooxy)-1,2-piperidinedicarboxylate 
• 133192-46-8 bis(phenylmethyl) cis-4-hydroxy-1,2-piperidinedicarboxylate 
• 133192-45-7 2-methyl 1-(phenylmethyl) cis-4-hydroxy-1,2-piperidinedicarboxylate 
• 3471-66-7 (2S,4R)-4-Hydroxy-piperidine-1,2-dicarboxylic acid 1-benzyl ester 

Relevant academic research and scientific papers

Bisubstrate inhibitors of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase: Transition state analogs for high affinity binding

6-Hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) is a key enzyme in the folate biosynthesis pathway. It catalyzes pyrophosphoryl transfer from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP). HPPK is essential for microorganisms but absent in mammals; therefore, it is an attractive target for developing novel antimicrobial agents. Previously, based on our studies of the structure and mechanism of HPPK, we created first-generation bisubstrate inhibitors by linking 6-hydroxymethylpterin to adenosine through phosphate groups, and developed second-generation inhibitors by replacing the phosphate bridge with a linkage that contains a piperidine moiety. Here, we report third-generation inhibitors designed based on the piperidine-containing inhibitor, mimicking the transition state. We synthesized two such inhibitors, characterized their protein-binding and enzyme inhibition properties, and determined their crystal structures in complex with HPPK, advancing the development of such bisubstrate analog inhibitors.

A facile synthesis of N-benzylallylglycine

N-Benzylallylglycine can be prepared in good yield through a one-pot reaction of N-benzylhomoallylamine with glyoxylic acid monohydrate in methanol. The reaction method described requires only mild conditions and avoids the need for purification of the amino acid product. (C) 2000 Elsevier Science Ltd.

HPPK INHIBITORS USEFUL AS ANTIBACTERIAL AGENTS

The disclosure provides linked purine pterin compounds of Formula I that are novel inhibitors of HPPK, a kinase responsible for an essential step in the biosynthesis of folic acid. (Formula I) The variables, e.g., A1-A3, R1-R4, B1-B2, and L1 are defined in the disclosure. These linked purine pterin inhibitors bind to HPPK with high affinity and specificity. Pharmaceutical compositions containing the HPPK inhibitors and methods of treating a bacterial infection in a patient with one or more of the HPPK inhibitors of the disclosure are also provided.

A cascade Aza-Cope/Aza-prins cyclization leading to piperidine derivatives

The cascade aza-Cope/aza-Prins cyclization of homoallylamines to give substituted piperidines has been explored. The use of glyoxalic acid as the carbonyl component afforded bicyclic structures as a result of the internal carboxylate anion trapping the intermediate cation. The unimolecular bis-, tris-, and tetrakis(homoallylamine)s efficiently delivered the appended bis-, tris- and tetrakis(piperidine-4-ol)s (tripod and crucifix shape, respectively) as new entities. The latter compound served as an excellent ligand in the Suzuki-Miyaura cross-coupling reaction to synthesize incrustoporin. The cascade aza-Cope/aza-Prins cyclization of homoallylamines to give substituted piperidines is described. A unimolecular tetrapiperidine derivative, which resulted from this strategy, was employed as a ligand in the Suzuki-Miyaura cross-coupling reaction of an α-iodobutenolide with an arylboronic acid in an efficient synthesis of incrustoporin and its analogues.