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Original Articles

Identification, Cloning, and Sequencing of the Genes Involved in the Conversion of D,L-2-Amino-Δ2-Thiazoline-4-Carboxylic Acid to …

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Pages 1097-1104 | Received 25 Dec 2001, Accepted 27 Dec 2001, Published online: 22 May 2014

  • 1) Sano, K., Yokozeki, Y., Tamura, F., Yasuda, N., Noda, I., and Mitsugi, K., Microbial conversion of D,L-2-amino-Δ2-thiazoline-4-carboxylic acid to L-cysteine and L-cystine: Screening of microorganisms and identification of products. Appl. Environ. Microbiol., 34, 806-810 (1977).
  • 2) Sano, K. and Mitsugi, K., Enzymatic production of L-cysteine from DL-2-amino-Δ2-thiazoline-4-carboxylic acid by Pseudomonas thiazolinophilum: Optimal conditions for the enzyme formation and enzymatic reaction. Agric. Biol. Chem., 42, 2315-2321 (1978).
  • 3) Sano, K., Eguchi, C., Yasuda, N., and Mitsugi, K., Metabolic pathway of L-cysteine formation from D,L-2-amino-Δ2-thiazoline-4-carboxylic acid by Pseudomonas. Agric. Biol. Chem., 43, 2373-2374 (1979).
  • 4) Ryu, O. H. and Shin, C. S., Analysis of the reaction steps in the bioconversion of D,L-ATC to L-cysteine. J. Microbiol. Biotechnol., 1, 50-53 (1991).
  • 5) Tamura, Y., Nishino, M., Ohmachi, T., and Asada, Y., N-Carbamoyl-L-cysteine as an intermediate in the bioconversion from D,L-2-amino-Δ2-thiazoline-4- carboxylic acid to L-cysteine by Pseudomonas sp. ON-4a. Biosci. Biotechnol. Biochem., 62, 2226-2229 (1998).
  • 6) Shiba, T. and Shiba, T., Japan Kokai Tokkyo Koho, 139476 (May 23, 2000).
  • 7) Sambrook, J., Fritsch, E. F., and Maniatis, T., In “Molecular cloning: A laboratory manual” 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York (1989).
  • 8) Hanahan, D., Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol., 166, 557-580 (1983).
  • 9) Wilson, K., Preparation of genomic DNA from bacteria. In “Current Protocols in molecular biology”, eds. Ausubel, F. M., Breut, R., Kingston, R. E., Moore, D. D., Seidman, J. D., Smith, J. A., and Struhl, K., John Wiley and Sons, New York, pp. 2.4.1-2.4.5 (1987).
  • 10) Henikoff, S., Unidirectional digestion with exonuclase III creates targeted breakpoints for DNA sequencing. Gene, 28, 351-359 (1984).
  • 11) Sanger, F., Nicklen, S., and Coulson, A. R., DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA, 74, 5463-5467 (1977).
  • 12) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature(London), 227, 680-685 (1970).
  • 13) Gaitonde, M. K., A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids. Biochem. J., 104, 627-633 (1967).
  • 14) States, B. and Segal, S., Quantitation of cyst(e)ine in human fibroblasts and separation of cysteinesulfinic acid, cysteic acid and taurine. Clin. Chem. Acta, 43, 49-53 (1973).
  • 15) Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265-275 (1951).
  • 16) Wilms, B., Wiese, A., Syldatk, C., Mattes, R., Altenbuchner, J., and Pietzsch, M., Cloning, nucleotide sequence and expression of a new L-N-carbamoylase gene from Arthrobacter aurescens DSM 3747 in E. coli.J. Biotechnol., 68, 101-113 (1999).
  • 17) Mukohara, Y., Ishikawa, T., Watanabe, K., and Nakamura, H., Molecular cloning and sequencing of the gene for a thermostable N-carbamyl-L-amino acid amidohydrolase from Bacillus stearothermophilus strain NS1122A. Biosci. Biotechnol. Biochem., 57, 1935-1937 (1993).
  • 18) Watanabe, K., Ishikawa, T., Mukohara, Y., and Nakamura, H., Cloning and sequencing of the genes involved in the conversion of 5-substituted hydantoins to the corresponding L-amino acids from the native plasmid of Pseudomonas sp. strain NS671. J. Bacteriol., 174, 962-969 (1992).
  • 19) Ogawa, J., Chug, M. C.-M., Hida, S., Yamada, H., and Shimizu, S., Thermostable N-carbamoyl-D- amino acid amidohydrolase: screening, purification and characterization. J. Biotechnol., 38, 11-19 (1994).
  • 20) Ikenaka, Y., Nanba, H., Yamada, Y., Yajima, K., Takano, M., and Takahashi, S., Screening, characterization, and cloning of the gene for N-carbamyl-D-amino acid amidohydrolase from thermotolerant soil bacteria. Biosci. Biotechnol. Biochem., 62, 882-886 (1998).
  • 21) Nanba, H., Ikenaka, Y., Yamada, Y., Yajima, K., Takano, M., and Takahashi, S., Isolation of Agrobacterium sp. strain KNK712 that produces N-carbamyl-D-amino acid amidohydrolase, cloning of the gene for this enzyme, and properties of the enzyme. Biosci. Biotechnol. Biochem., 62, 875-881 (1998).
  • 22) Syldatk, C., Muhler, R., Pietzsch, M., and Wagner, F., Microbial and enzymatic production of L-amino acids from DL-5-monosubstituted hydantoins. In “Biocatalytic production of amino acids and derivatives”, eds. Rozzell, J. D. and Wagner, F., Hanser Publishers, New York, pp. 129-176 (1992).
  • 23) Ishikawa, T., Watanabe, K., Mukohara, Y., Kobayashi, S., and Nakamura, H., Microbial conversion of DL-5-substituted hydantoins to the corresponding L-amino acids by Pseudomonas sp. strain NS671. Biosci. Biotechnol. Biochem., 57, 982-986 (1993).
  • 24) Ishikawa, T., Watanabe, K., Mukohara, Y., and Nakamura, H., N-Carbamyl-L-amino acid amidohydrolase of Pseudomonas sp. strain NS671: Purification and some properties of the enzyme expressed in Escherichia coli.Biosci. Biotechnol. Biochem., 60, 612-615 (1996).
  • 25) Ogawa, J., Shimizu, S., and Yamada, H., N- Carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c. Purification and characterization. Eur. J. Biochem., 212, 685-691 (1993).
  • 26) Ogawa, J., Miyake, H., and Shimizu, S., Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans.Appl. Microbiol. Biotechnol., 43, 1039-1043 (1995).
  • 27) LaPointe, G., Viau, S., Leblanc, D., Robert, N. and Morin, A., Cloning, sequencing, and expression in Escherichia coli of the D-hydantoinase gene from Pseudomonas putida and distribution of homologous genes in other microorganisms. Appl. Environ. Microbiol., 60, 888-895 (1994).

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