In organic chemistry, atoms other than carbon and hydrogen are generally referred to as heteroatoms. The most common heteroatoms are nitrogen, oxygen and sulfur. Now I present to you an article called The stability of L-ATC hydrolase participating in L-cysteine production, published in 1995-03-31, which mentions a compound: 2150-55-2, mainly applied to aminothiazolinecarboxylate hydrolase stabilization cysteine manufacture, Application In Synthesis of 2-Amino-4,5-dihydrothiazole-4-carboxylic acid.
In the production of L-cysteine from DL-2-amino-Δ2-thiazoline-4-carboxylic acid (DL-ATC), the stability of the relevant enzymes produced by Pseudomonas sp. was tested, and strategies to improve the stability of L-ATC hydrolase were investigated with respect to water activity and ionic strength. Among the 3 enzymes which participate in L-cysteine production, i.e., ATC racemase, L-ATC hydrolase, and S-carbamyl-L-cysteine hydrolase, L-ATC hydrolase is the least stable. Various mixtures of salts and sorbitol were added to adjust the water activities of the tested solutions As the water activity decreased from 0.93 to 0.80, the stability of L-ATC hydrolase was sharply enhanced. In the absence of sorbitol, the stability of L-ATC hydrolase increased in proportion to ionic strength. Even though enzyme stability was not good at a low ionic strength, it was enhanced by lowering the water activity with the addition of sorbitol. The half-life of L-ATC hydrolase in sorbitol-salt mixtures increased by 10- to 20-fold compared to that of a control.
From this literature《The stability of L-ATC hydrolase participating in L-cysteine production》,we know some information about this compound(2150-55-2)Application In Synthesis of 2-Amino-4,5-dihydrothiazole-4-carboxylic acid, but this is not all information, there are many literatures related to this compound(2150-55-2).