88291-62-7

Upstream product

• 67-56-1 methanol 
• 4896-75-7 <2-2H2>glycine 

Downstream Products

• 139879-19-9 methyl <2-²H₂>-N-(2,3-dihydroxybenzoyl)glycinate 

Relevant academic research and scientific papers

DEUTERATED BENZIMIDAZOLE COMPOUND AND MEDICAL USE THEREOF

The present invention relates to a medicament for treating or preventing a disease involving Na channel, for example, neuropathic pain, nociceptive pain, inflammatory pain, small-fiber neuropathy, erythromelalgia, paroxysmal extreme pain disorder, dysuria, or multiple sclerosis, comprising a compound of formula (I) wherein R1a, R1b, R1c, and R1d are hydrogen, halogen, cyano, C1-4 alkyl, C1-4 alkoxy, etc., provided that at least one of R1a, R1b, R1c and R1d is the above C6-10 aryl, C6-10 aryloxy, etc., R2 and R3 are hydrogen, C1-6 alkyl, C3-10 cycloalkyl, etc., R4 is hydrogen, C1-6 alkyl, C3-7 cycloalkyl, etc., m is 0, 1, or 2, L is CR7R8, R7 and R8 are hydrogen, hydroxy group, C1-4 alkyl, C1-4 alkoxy, etc., or a pharmaceutically acceptable salt thereof.

The Stereochemical Course of Decarboxylation, Transamination and Elimination Reactions Catalysed by Escherichia coli Glutamic Acid Decarboxylase

Pyridoxal 5'-phosphate dependent Escherichia coli glutamic acid decarboxylase reprotonates the quinonoid intermediate derived from the coenzyme and its natural substrate, (2S)-glutamic acid on the 4'-Si-face of the coenzyme during an abortive decarboxylation-transamination reaction.The enzyme introduces the 3-pro-R hydrogen of β-alanine with retention of configuration during the decarboxylation of (2S)-aspartic acid.In the absence of pyridoxal 5'-phosphate, treatment of the inactive apoenzyme with the inhibitor N4'-(2"-phosphoethyl)pyridoxamine 5'-phosphate results in reactivation through the formation of the active pyridoxal 5'-phosphate holoenzyme complex.During this reaction hydrogen phosphate is eliminated from the phosphoethyl moiety.Using synthetic chirally deuteriated isotopomers of the inhibitor it is demonstrated that the 1-pro-R hydrogen of inhibitor is removed during the reactivation reaction.The results suggest that protonations and deprotonations at Cα of quinonoid intermediates derived from the coenzyme and the substrate occur from the 4'-Si-face of the coenzyme and that the distal binding groups of the substrates and inhibitors occupy similar positions at the active site on the 3'-phenolic group side of the coenzyme.

Biosynthesis of the Antibiotic Obafluorin from p-Aminophenylalanine and Glycine (Glyoxylate)

Results of experiments using 'resting' cells of Pseudomonas fluorescens with -, - and 2H2>-glycine as precursors show that glyoxylic acid is specifically the source of C-1 and C-2 of the antibiotic obafluorin 1.The 13C labelling patterns are consistent with the passage of the precursors through the tartronic semialdehyde and glyoxylate pathways.The glycine derivative 6 is not a precursor for 1.The analogues 24 and 25 of p-aminophenylalanine 3 are synthesised and tested as substrates for biosynthesis in P. fluorescens.With 24, the metabolite 26 is detected; no metabolites of 25 are detected.