26081-02-7

Upstream product

• 16935-34-5 5-isopropyl-imidazolidine-2,4-dione 
• 40856-74-4 (5S)-5-(propan-2-yl)imidazolidine-2,4-dione 

Downstream Products

• 1118428-85-5 C₂₄H₂₈N₄O₄ 
• 1118428-84-4 C₂₄H₂₈N₄O₄ 
• 16935-34-5 5-isopropyl-imidazolidine-2,4-dione 
• 1529780-93-5 1-isobutyl-5-phenylpyrimidin-2(1H)-one 
• 1529780-92-4 (2S)-3-methyl-2-((E)-3-(3-oxo-2-phenylpropylidene)ureido)butyric acid 
• 258833-80-6 (S)-2-[3-((R)-1-Benzyloxycarbonylamino-2-hydroxy-ethyl)-pyrazol-1-yl]-3-methyl-butyric acid methyl ester 
• 258833-68-0 (S)-2-[5-((R)-1-Benzyloxycarbonylamino-2-hydroxy-ethyl)-pyrazol-1-yl]-3-methyl-butyric acid methyl ester 
• 258830-58-9 (R)-4-[1-((S)-1-Carboxy-2-methyl-propyl)-1H-pyrazol-3-yl]-oxazolidine-3-carboxylic acid benzyl ester 
• 258830-46-5 (R)-4-[2-((S)-1-Carboxy-2-methyl-propyl)-2H-pyrazol-3-yl]-oxazolidine-3-carboxylic acid benzyl ester 
• 461-72-3 2,4-imidazolidinedione 
• 40856-74-4 (5S)-5-(propan-2-yl)imidazolidine-2,4-dione 
• 686-43-1 valylglycine 
• 72-18-4 L-valine 

Relevant academic research and scientific papers

Mechanism of Stereospecific Production of L-Amino Acids from the Corresponding 5-Substituted Hydantoins by Bacillus brevis

The mechanism of stereospecific production of L-amino acids from the corresponding 5-substituted hydantoins by Bacillus brevis AJ-12299 was studied.The enzymes involved in the reaction were partially purified by DEAE-Toyopearl 650M column chromatography and their properties were investigated.The conversion of DL-5-substituted hydantoins to the corresponding L-amino acids consisted of the following two successive reactions.The first step was the ring-opening hydrolysis to N-carbamoyl amino acids catalyzed by an ATP dependent L-5-substituted hydantoin hydrolase.This reaction was stereospecific and the N-carbamoyl amino acid produced was exclusively the L-form.N-Carbamoyl-L-amino acid was also produced from the D-form of 5-substituted hydantoin, which suggests that spontaneous racemization occurred in the reaction mixture.In the second step, N-carbamoyl-L-amino acid was hydrolyzed to L-amino acid by an N-carbamoyl-L-amino acid hydrolase, which was also an L-specific enzyme.The ATP dependency of the L-5-substituted hydantoin hydrolase was supposed to be the limiting factor in the production of L-amino acids from the corresponding 5-substituted hydantoins by this bacterium.

Enzymatic Production of L-Amino Acids from the Corresponding 5-Substituted Hydantoins by a Newly Isolated Bacterium, Bacillus brevis AJ-12299

A bacterium that stereospecifically produces L-valine from 5-isopropylhydantoin was isolated from soil.It was identified as Bacillus brevis and given the number AJ-12299.L-Valine productivity from L-, D- or DL-5-isopropylhydantoin by B. brevis AJ-12299 was rather low beacuse this bacterium had L-valine degrading-activity.In contrast, the productivity was improved by a mutant the L-valine degradation pathway of which was genetically blocked, and the 5-isopropylhydantoin consumed was stoichiometrically converted to L-valine.The optimal temperature and pH of the reaction were 30 deg C and 7.0 ca. 7.5.The enzyme involved in the reaction was inducible and was strongly induced by the addition of 5-isopropylhydantoin.In addition to L-valine production, this bacterium also produced various aliphatic and aromatic L-amino acids from the corresponding 5-substituted hydantoins.