Substrate and stereochemical specificity of the organophosphorus acid anhydrolase from Alteromonas sp. JD6.5 toward p -nitrophenyl phosphotriesters

Substrate and stereochemical specificity of the organophosphorus acid anhydrolase from Alteromonas sp. JD6.5 toward p -nitrophenyl phosphotriesters Paraoxon, 4-nitrophenyl phosphate and acetate are substrates of α- but not of β-, γ- and ζ-carbonic anhydrases Structure–activity relationship on human serum paraoxonase (PON1) using substrate analogues and inhibitors Stereospecific cholinesterase inhibition by O , S -diethylphenylphosphonothioate Substrate specificity of immobilized penicillin-G acylase towards penicillin and cephalosporin derivatives was studied. The phenylacetyl moiety can be altered at the α-position with several small substituents. Depending on polarity and size of the substituent, enzyme activity decreases or increases. Insertion or deletion of atoms between the aromatic nucleus of the phenylacetyl group and the center of hydrolysis leads to substrates that are no longer recognized by the enzyme. Synthesis and anti-acetylcholinesterase properties of novel β- and γ-substituted alkoxy organophosphonates Substrate Specificity and Stereoselectivity of Rat Brain Microsomal Anandamide Amidohydrolase Phospholipase A2-like catalytic antibody Pyridoacridine alkaloids from deep-water marine sponges of the family Pachastrellidae: structure revision of dercitin and related compounds and correlation with the kuanoniamines The New Metabolite (<i>S</i>)‐Cinnamoylphosphoramide from<i>Streptomyces</i>sp. and Its Total Synthesis