메뉴 건너뛰기




Volumn 65, Issue 6, 2004, Pages 686-693

A novel M-carbamoyl-L-amino acid amidohydrolase of Pseudomonas sp. strain ON-4a: Purification and characterization of M-carbamoyl-L-cysteine amidohydrolase expressed in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COLUMN CHROMATOGRAPHY; ELECTROPHORESIS; ENZYME INHIBITION; ESCHERICHIA COLI; GELS; GENES; HYDROLYSIS; PURIFICATION; SUBSTRATES;

EID: 8644265009     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-004-1687-2     Document Type: Article
Times cited : (15)

References (35)
  • 1
    • 0030952237 scopus 로고    scopus 로고
    • Two amino acid amidohydrolase genes encoding L-stereospecific carbamoylase and aminoacylase are organized in a common operon in Bacillus stearothermophilus
    • Batisse N, Weigel P, Lecocq M, Sakanyan V (1997) Two amino acid amidohydrolase genes encoding L-stereospecific carbamoylase and aminoacylase are organized in a common operon in Bacillus stearothermophilus. Appl Environ Microbiol 63:763-766
    • (1997) Appl Environ Microbiol , vol.63 , pp. 763-766
    • Batisse, N.1    Weigel, P.2    Lecocq, M.3    Sakanyan, V.4
  • 2
    • 0014118789 scopus 로고
    • A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids
    • Gaitonde MK (1967) A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids. Biochem J 104:627-633
    • (1967) Biochem J , vol.104 , pp. 627-633
    • Gaitonde, M.K.1
  • 3
    • 0037399175 scopus 로고    scopus 로고
    • Characterization and phylogenetic analysis of a thermostable N-carbamoyl-L-amino acid amidohydrolase from Bacillus kaustophilus CCRC11223
    • Hu H-Y, Hsu W-H, Chien HR (2003) Characterization and phylogenetic analysis of a thermostable N-carbamoyl-L-amino acid amidohydrolase from Bacillus kaustophilus CCRC11223. Arch Microbiol 179:250-257
    • (2003) Arch Microbiol , vol.179 , pp. 250-257
    • Hu, H.-Y.1    Hsu, W.-H.2    Chien, H.R.3
  • 4
    • 0002541792 scopus 로고
    • Degradation of amino acids accompanying in vitro protein hydrolysis
    • Barrett GC (ed) Chapman & Hall, London
    • Hunt S (1985) Degradation of amino acids accompanying in vitro protein hydrolysis. In: Barrett GC (ed) Chemistry and biochemistry of the amino acids. Chapman & Hall, London, pp 376-398
    • (1985) Chemistry and Biochemistry of the Amino Acids , pp. 376-398
    • Hunt, S.1
  • 5
    • 0002541792 scopus 로고
    • Degradation of amino acids accompanying in vitro protein hydrolysis
    • Barrett GC (ed) Chapman & Hall, London
    • Hunt S (1985) Degradation of amino acids accompanying in vitro protein hydrolysis. In: Barrett GC (ed) Chemistry and biochemistry of the amino acids. Chapman & Hall, London, pp 376-398
    • (1985) Chemistry and Biochemistry of the Amino Acids , pp. 376-398
    • Hunt, S.1
  • 6
    • 0032061344 scopus 로고    scopus 로고
    • Screening, characterization, and cloning of the gene for N-carbamyl-D-amino acid amidohydrolase from thermotolerant soil bacteria
    • Ikenaka Y, Nanba H, Yamada Y, Yajima K, Takano M, Takahashi S (1998) 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) Biosci Biotechnol Biochem , vol.62 , pp. 882-886
    • Ikenaka, Y.1    Nanba, H.2    Yamada, Y.3    Yajima, K.4    Takano, M.5    Takahashi, S.6
  • 7
    • 0000831186 scopus 로고
    • Microbial conversion of DL-5-substituted hydantoins to the corresponding L-amino acids by Pseudomonas sp. strain NS671
    • Ishikawa T, Watanabe K, Mukohara Y, Kobayashi S, Nakamura H (1993) 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) Biosci Biotechnol Biochem , vol.57 , pp. 982-986
    • Ishikawa, T.1    Watanabe, K.2    Mukohara, Y.3    Kobayashi, S.4    Nakamura, H.5
  • 8
    • 0028011156 scopus 로고
    • Microbial conversion of DL-5-substituted hydantoins to the corresponding L-amino acids by Bacillus stearothermophilus NS1122A
    • Ishikawa T, Mukohara Y, Watabe K, Kobayashi S, Nakamura H (1994) Microbial conversion of DL-5-substituted hydantoins to the corresponding L-amino acids by Bacillus stearothermophilus NS1122A. Biosci Biotechnol Biochem 58:265-270
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 265-270
    • Ishikawa, T.1    Mukohara, Y.2    Watabe, K.3    Kobayashi, S.4    Nakamura, H.5
  • 9
    • 0030118058 scopus 로고    scopus 로고
    • N-Carbmyl-L-amino acid amidohydrolase of Pseudomonas sp. strain NS671: Purification and some properties of the enzyme expressed in Escherichia coli
    • Ishikawa T, Watanabe K, Mukohara Y, Nakamura H (1996) N-Carbmyl-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) Biosci Biotechnol Biochem , vol.60 , pp. 612-615
    • Ishikawa, T.1    Watanabe, K.2    Mukohara, Y.3    Nakamura, H.4
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 85007856311 scopus 로고
    • Molecular cloning and sequencing of the thermostable N-carbamyl-L-amino acid amidohydrolase from Bacillus stearothermophilus strain NS 1122A
    • Mukohara Y, Ishikawa T, Watanabe K, Nakamura H (1993) Molecular cloning and sequencing of the thermostable N-carbamyl-L-amino acid amidohydrolase from Bacillus stearothermophilus strain NS 1122A. Biosci Biotechnol Biochem 57:1935-1937
    • (1993) Biosci Biotechnol Biochem , vol.57 , pp. 1935-1937
    • Mukohara, Y.1    Ishikawa, T.2    Watanabe, K.3    Nakamura, H.4
  • 13
    • 0032062635 scopus 로고    scopus 로고
    • 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
    • Nanba H, Ikenaka Y, Ymada Y, Yajima K, Takano M, Takahashi S (1998) 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) Biosci Biotechnol Biochem , vol.62 , pp. 875-881
    • Nanba, H.1    Ikenaka, Y.2    Ymada, Y.3    Yajima, K.4    Takano, M.5    Takahashi, S.6
  • 14
    • 0028168717 scopus 로고
    • Ureidopropionase with N-carbamoy-1-α-L-amino acid amidohydrolase activity from an aerobic bacterium, Pseudomonas putida IFO 12996
    • Ogawa J, Shimizu S (1994) β-Ureidopropionase with N-carbamoy-1-α-L-amino acid amidohydrolase activity from an aerobic bacterium, Pseudomonas putida IFO 12996. Eur J Biochem 223:625-630
    • (1994) Eur J Biochem , vol.223 , pp. 625-630
    • Ogawa, J.1    Shimizu, S.2
  • 15
    • 0027483420 scopus 로고
    • N-Carbamoly-D-amino acid amidohydrolase from Comamonas sp. E222c. Purification and characterization
    • Ogawa J, Shimizu S, Yamada H (1993) N-Carbamoly-D-amino acid amidohydrolase from Comamonas sp. E222c. Purification and characterization. Eur J Biochem 212:685-691
    • (1993) Eur J Biochem , vol.212 , pp. 685-691
    • Ogawa, J.1    Shimizu, S.2    Yamada, H.3
  • 16
    • 0028533605 scopus 로고
    • Thermostable N-carbamoyl-D-amino acid amidohydrolase: Screening, purification and characterization
    • Ogawa J, Chung MC-M, Hida S, Yamada H, Shimizu S (1994) Thermostable N-carbamoyl-D-amino acid amidohydrolase: screening, purification and characterization. J Biotechnol 38:11-19
    • (1994) J Biotechnol , vol.38 , pp. 11-19
    • Ogawa, J.1    Chung, M.C.-M.2    Hida, S.3    Yamada, H.4    Shimizu, S.5
  • 17
    • 0028805827 scopus 로고
    • Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans
    • Ogawa J, Miyake H, Shimizu S (1995) Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans. Appl Microbiol Biotechnol 43:1039-1043
    • (1995) Appl Microbiol Biotechnol , vol.43 , pp. 1039-1043
    • Ogawa, J.1    Miyake, H.2    Shimizu, S.3
  • 19
    • 0006896287 scopus 로고
    • Analysis of the reaction steps in the bioconversion of D,L-ATC to L-cysteine
    • Ryu OH, Shin CS (1991) Analysis of the reaction steps in the bioconversion of D,L-ATC to L-cysteine. J Microbiol Biotechnol 1:50-53
    • (1991) J Microbiol Biotechnol , vol.1 , pp. 50-53
    • Ryu, O.H.1    Shin, C.S.2
  • 20
    • 0343580527 scopus 로고    scopus 로고
    • Continous L-cysteine production using immobilized cell reactors and product extractors
    • Ryu OH, Yeong J, Shin CS (1997) Continous L-cysteine production using immobilized cell reactors and product extractors. Process Biochem 32:201-209
    • (1997) Process Biochem , vol.32 , pp. 201-209
    • Ryu, O.H.1    Yeong, J.2    Shin, C.S.3
  • 23
    • 0000112769 scopus 로고
    • 2- thiazoline-4-carboxylic acid by Pseudomonas thiazolinophilum: Optimal conditions for the enzyme formation and enzymatic reaction
    • 2-thiazoline-4-carboxylic acid by Pseudomonas thiazolinophilum: optimal conditions for the enzyme formation and enzymatic reaction. Agric Biol Chem 42:2315-2321
    • (1978) Agric Biol Chem , vol.42 , pp. 2315-2321
    • Sano, K.1    Mitsugi, K.2
  • 27
    • 0015918906 scopus 로고
    • Quantitation of cyst(e)ine in human fibroblasts and separation of cysteinesulfinic acid, cysteic acid and taurine
    • States B, Segal S (1973) Quantitation of cyst(e)ine in human fibroblasts and separation of cysteinesulfinic acid, cysteic acid and taurine. Clin Chem Acta 43:49-53
    • (1973) Clin Chem Acta , vol.43 , pp. 49-53
    • States, B.1    Segal, S.2
  • 28
    • 0002548361 scopus 로고
    • Microbial and enzymatic production of L-amino acids from DL-5-monosubstituted hydantoins
    • Rozzell JD, Wagner F (eds) Hanser, New York
    • Syldatk C, Muhler R, Pietzsch M, Wagner F (1992) Microbial and enzymatic production of L-amino acids from DL-5-monosubstituted hydantoins. In: Rozzell JD, Wagner F (eds) Biocatalytic production of amino acids and derivertives. Hanser, New York, pp 129-176
    • (1992) Biocatalytic Production of Amino Acids and Derivertives , pp. 129-176
    • Syldatk, C.1    Muhler, R.2    Pietzsch, M.3    Wagner, F.4
  • 29
    • 0002548361 scopus 로고
    • Microbial and enzymatic production of L-amino acids from DL-5-monosubstituted hydantoins
    • Rozzell JD, Wagner F (eds) Hanser, New York
    • Syldatk C, Muhler R, Pietzsch M, Wagner F (1992) Microbial and enzymatic production of L-amino acids from DL-5-monosubstituted hydantoins. In: Rozzell JD, Wagner F (eds) Biocatalytic production of amino acids and derivertives. Hanser, New York, pp 129-176
    • (1992) Biocatalytic Production of Amino Acids and Derivertives , pp. 129-176
    • Syldatk, C.1    Muhler, R.2    Pietzsch, M.3    Wagner, F.4
  • 32
    • 0000325980 scopus 로고
    • Mechanism of stereospecific production of L-amino acids from the corresponding 5-monosubstituted hydantoins by Bacillus brevis
    • Yamashiro K, Kubota K, Yokozeki K (1988) Mechanism of stereospecific production of L-amino acids from the corresponding 5-monosubstituted hydantoins by Bacillus brevis. Agric Biol Chem 52:2857-2863
    • (1988) Agric Biol Chem , vol.52 , pp. 2857-2863
    • Yamashiro, K.1    Kubota, K.2    Yokozeki, K.3
  • 33
    • 84951602838 scopus 로고
    • Mechanism of the asymmetric production of L-aromatic amino acids from the corresponding hydantoins by Flavobacterium spec.
    • Yokozeki K, Hirose Y, Kubota K (1987) Mechanism of the asymmetric production of L-aromatic amino acids from the corresponding hydantoins by Flavobacterium spec. Agric Biol Chem 51:737-746
    • (1987) Agric Biol Chem , vol.51 , pp. 737-746
    • Yokozeki, K.1    Hirose, Y.2    Kubota, K.3
  • 34
    • 0026508916 scopus 로고
    • 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 Pseudomonassp. strain NS671
    • Watanabe K, Ishikawa T, Mukohara Y, Nakamura H (1992) 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 Pseudomonassp. strain NS671. J Bacteriol 174:962-969
    • (1992) J Bacteriol , vol.174 , pp. 962-969
    • Watanabe, K.1    Ishikawa, T.2    Mukohara, Y.3    Nakamura, H.4
  • 35
    • 0032996229 scopus 로고    scopus 로고
    • Cloning, nucleotide sequence and expression of a new L-carbamoylase gene from Arthrobacter aurescens DSM3747 in E. coli
    • Wilms B, Wiese A, Syldatk C, Mattes R, Altenbuchner J, Pietzsch M (1999) Cloning, nucleotide sequence and expression of a new L-carbamoylase gene from Arthrobacter aurescens DSM3747 in E. coli. J Biotechnol 68:101-113
    • (1999) J Biotechnol , vol.68 , pp. 101-113
    • Wilms, B.1    Wiese, A.2    Syldatk, C.3    Mattes, R.4    Altenbuchner, J.5    Pietzsch, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.