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Volumn 63, Issue 2, 1997, Pages 763-766

Two amino acid amidohydrolase genes encoding L-stereospecific carbamoylase and aminoacylase are organized in a common operon in Bacillus stearothermophilus

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; GENE LOCATION; GENE ORDER; GEOBACILLUS STEAROTHERMOPHILUS; MOLECULAR CLONING; NONHUMAN; OPERON; SEQUENCE ANALYSIS; TRANSCRIPTION INITIATION;

EID: 0030952237     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.63.2.763-766.1997     Document Type: Article
Times cited : (15)

References (16)
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  • 3
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  • 4
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    • Use of the overexpressed Bacillus stearothermophilus aminoacylase for the resolution of D,L-amino acids in conventional and non-conventional media
    • Dion, M., F. Loussouarn, N. Batisse, C. Rabiller, and V. Sakanyan. 1995. Use of the overexpressed Bacillus stearothermophilus aminoacylase for the resolution of D,L-amino acids in conventional and non-conventional media. Biotechnol. Lett. 17:905-910.
    • (1995) Biotechnol. Lett. , vol.17 , pp. 905-910
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  • 6
    • 0029160754 scopus 로고
    • Thermostable D-hydantoinase from thermophilic Bacillus stearothermophilus SD-1: Characteristics of purified enzyme
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    • (1995) Appl. Microbiol. Biotechnol. , vol.43 , pp. 270-276
    • Lee, S.-G.1    Lee, D.-C.2    Hong, S.-P.3    Sung, M.-H.4    Kim, H.-S.5
  • 7
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    • Effect of the nitrogen source on phycobiliprotein synthesis and cell reserves in a chromatically adapting filamentous cyanobacterium
    • Liotenberg, S., D. Campbell, R. Rippka, J. Houmard, and N. Tandeau de Marsac. 1996. Effect of the nitrogen source on phycobiliprotein synthesis and cell reserves in a chromatically adapting filamentous cyanobacterium. Microbiology 142:611-622.
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  • 8
    • 85007856311 scopus 로고
    • Molecular cloning and sequencing of the gene for a thermostable N-carbamyl-L-amino acid amidohydrolase from Bacillus stearothermophilus strain NS1122A
    • Mukohara, Y., T. Ishikawa, K. Watabe, and H. Nakamura. 1993. 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) Biosci. Biotechnol. Biochem. , vol.57 , pp. 1935-1937
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  • 10
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    • β-Urcidopropionase with N-carbamoyl-α-L-amino acid amidohydrolase activity from an aerobic bacterium. Pseudomonas putida IFO12996
    • Ogawa, J., and S. Shimizu. 1994. β-Urcidopropionase with N-carbamoyl-α-L-amino acid amidohydrolase activity from an aerobic bacterium. Pseudomonas putida IFO12996. Eur. J. Biochem. 293:625-630.
    • (1994) Eur. J. Biochem. , vol.293 , pp. 625-630
    • Ogawa, J.1    Shimizu, S.2
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    • A re-examination of the pathway for ornithine biosynthesis in a thermophilic and two mesophilic Bacillus species
    • Sakanyan, V., A. Kochikyan, I. Mett, C. Legrain, D. Charlier, A. Piérard, and N. Glansdorff. 1992. A re-examination of the pathway for ornithine biosynthesis in a thermophilic and two mesophilic Bacillus species. J. Gen. Microbiol. 138:125-130.
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  • 15
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    • (1992) Biocatalytic Production of Amino Acids and Derivatives , pp. 129-176
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  • 16
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.