Ohmachi, Tetsuo; Nishino, Mizuka; Kawata, Maki; Edo, Namiko; Funaki, Hiroko; Narita, Megumi; Mori, Kazuyuki; Tamura, Yoshiharu; Asada, Yoshihiro published an article about the compound: 2-Amino-4,5-dihydrothiazole-4-carboxylic acid( cas:2150-55-2,SMILESS:O=C(C1N=C(N)SC1)O ).Product Details of 2150-55-2. Aromatic heterocyclic compounds can be classified according to the number of heteroatoms or the size of the ring. The authors also want to convey more information about this compound (cas:2150-55-2) through the article.
The newly isolated strain Pseudomonas sp. ON-4a converts D,L-2-amino-Δ2-thiazoline-4-carboxylic acid (D,L-ATC) to L-cysteine via N-carbamoyl-L-cysteine. A genomic DNA fragment from this strain containing the gene(s) encoding enzymes that convert D,L-ATC into L-cysteine was cloned in Escherichia coli. Transformants expressing cysteine-forming activity were selected by growth of an E. coli mutant defective in the cysB gene. A pos. clone, denoted CM1, carrying the plasmid pCM1 with an insert DNA of approx. 3.4 kb was obtained, and the nucleotide sequence of a complementing region was analyzed. Anal. of the sequence found two open reading frames, ORF1 and ORF2, which encoded proteins of 183 and 435 amino acid residues, resp. E. coli DH5α harboring pTrCM1, which was constructed by inserting the subcloned sequence into an expression vector, expressed two proteins of 25 kDa and 45 kDa. From the analyses of crude extracts of E. coli DH5α carrying deletion derivatives of pTrCM1 by sodium dodecyl sulfatepolyacrylamide gel electrophoresis and by enzymic activity, it was found that the 25-kDa protein encoded by ORF1 was the enzyme L-2-amino-Δ2-thiazoline-4-carboxylic acid hydrolase, which catalyzes the conversion of D,L-ATC to N-carbamoyl-L-cysteine, and that the 45-kDa protein encoded by ORF2 was the enzyme N-carbamoyl-L-cysteine amidohydrolase, which catalyzes the conversion of N-carbamoyl-L-cysteine to L-cysteine.
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