Epoxy compounds usually have stronger nucleophilic ability, because the alkyl group on the oxygen atom makes the bond angle smaller, which makes the lone pair of electrons react more dissimilarly with the electron-deficient system. Compound: 2-Amino-4,5-dihydrothiazole-4-carboxylic acid, is researched, Molecular C4H6N2O2S, CAS is 2150-55-2, about Effects of anoxic conditions on the enzymic conversion of DL-2-aminothiazoline-4-carboxylic acid to L-cystine.Application of 2150-55-2.
The effects of anoxic conditions on product inhibition and the stability of L-2-aminothiazoline-4-carboxylic acid (L-ATC) hydrolase were investigated in the conversion of DL-2-amino-Δ2-thiazoline-4-carboxylic acid (DL-ATC) to L-cystine (I) using the cell-free extract enzyme of Pseudomonas sp. in the presence of hydroxylamine. At L-cysteine (II) equivalent levels (I:II = 1:2), I inhibited the L-ATC hydrolase reaction to a greater extent than II. In air, the product occurred predominantly as I (94.9%), whereas in a N2 atm. the product occurred as a mixture of II (39.3%) and I (40.7%). Less product inhibition took place in N. The activity of L-ATC hydrolase was almost fully lost after 20 h of incubation by shaking at 30° in air, but considerable activity remained under the anoxic conditions of N2. A kinetic anal. of the reactions confirmed that reduced product inhibition and enhanced enzyme stability in N2 result in a more efficient enzyme reaction. The inactivation rate constant (k1) was estimated to be 0.11/h in N2 and 0.22/h in air, indicating that the stability of L-ATC hydrolase in N2 was greater than in air. The values of the Kp1 and Kp2 constants related to product inhibition were 43.36 mM and 30.48 mM for II and I, resp., where higher values were an indication of less product inhibition. The value of the rate constant (k2) for the oxidation of II to I was 0.09/h in N2 and 1.01/h in air, suggesting that the II oxidation to I proceeds faster in air than in N2.
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