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Volumn 228, Issue 1, 2003, Pages 1-9

Genes for an alkaline D-stereospecific endopeptidase and its homolog are located in tandem on Bacillus cereus genome

Author keywords

Bacillus cereus; D Phenylalanine oligopeptide; D Stereospecific endopeptidase; Tandem location

Indexed keywords

ALKALINE DEXTRO PEPTIDASE; ALKALINE DEXTRO PEPTIDASE 2; ALKALINE PROTEINASE; BACTERIAL ENZYME; DEXTRO PHENYLALANINAMINE; DEXTRO PHENYLALANINE 3; DEXTRO PHENYLALANINE 4; DEXTRO PHENYLALANINE 6; DNA FRAGMENT; PHENYLALANINAMINE; PHENYLALANINE 4; PHENYLALANINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0242552667     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(03)00665-7     Document Type: Article
Times cited : (8)

References (31)
  • 1
    • 0034071105 scopus 로고    scopus 로고
    • Enzymes acting on peptides containing D-amino acid
    • Asano Y., Lübbehüsen T.L. Enzymes acting on peptides containing D-amino acid. J. Biosci. Bioeng. 89:2000;295-306.
    • (2000) J. Biosci. Bioeng. , vol.89 , pp. 295-306
    • Asano, Y.1    Lübbehüsen, T.L.2
  • 3
    • 0032472314 scopus 로고    scopus 로고
    • Industrial biotransformations for the production of D-amino acids
    • Yagasaki M., Ozaki A. Industrial biotransformations for the production of D-amino acids. J. Mol. Catal. B. 4:1998;1-11.
    • (1998) J. Mol. Catal. B , vol.4 , pp. 1-11
    • Yagasaki, M.1    Ozaki, A.2
  • 4
    • 0019781513 scopus 로고
    • Microbial transformation of racemic hydantoins to D-amino acids
    • Olivieri R., Fascetti E., Angelini L., Degen L. Microbial transformation of racemic hydantoins to D-amino acids. Biotechnol. Bioeng. 23:1981;2173-2183.
    • (1981) Biotechnol. Bioeng. , vol.23 , pp. 2173-2183
    • Olivieri, R.1    Fascetti, E.2    Angelini, L.3    Degen, L.4
  • 5
    • 0024393970 scopus 로고
    • Properties of a novel D-stereospecific aminopeptidase from Ochrobactrum anthropi
    • Asano Y., Nakazawa A., Kato Y., Kondo K. Properties of a novel D-stereospecific aminopeptidase from Ochrobactrum anthropi. J. Biol. Chem. 264:1989;14233-14239.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14233-14239
    • Asano, Y.1    Nakazawa, A.2    Kato, Y.3    Kondo, K.4
  • 6
    • 0026526120 scopus 로고
    • Structural similarity of D-aminopeptidase to carboxypeptidase DD and β-lactamases
    • Asano Y., Kato Y., Yamada A., Kondo K. Structural similarity of D-aminopeptidase to carboxypeptidase DD and β-lactamases. Biochemistry. 31:1992;2316-2328.
    • (1992) Biochemistry , vol.31 , pp. 2316-2328
    • Asano, Y.1    Kato, Y.2    Yamada, A.3    Kondo, K.4
  • 8
    • 0034067403 scopus 로고    scopus 로고
    • Gene cloning, nucleotide sequencing, and purification and characterization of the D-stereospecific amino-acid amidase from Ochrobactrum anthropi SV3
    • Komeda H., Asano Y. Gene cloning, nucleotide sequencing, and purification and characterization of the D-stereospecific amino-acid amidase from Ochrobactrum anthropi SV3. Eur. J. Biochem. 267:2000;2028-2035.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2028-2035
    • Komeda, H.1    Asano, Y.2
  • 9
    • 84990076462 scopus 로고
    • Discovery of a D-stereospecific aminopeptidase and its use as a catalyst in organic synthesis
    • Asano Y., Nakazawa A., Kato Y., Kondo K. Discovery of a D-stereospecific aminopeptidase and its use as a catalyst in organic synthesis. Angew. Chem. Int. Ed. Engl. 28:1989;450-451.
    • (1989) Angew. Chem. Int. Ed. Engl. , vol.28 , pp. 450-451
    • Asano, Y.1    Nakazawa, A.2    Kato, Y.3    Kondo, K.4
  • 11
    • 0001635545 scopus 로고
    • First stereoselective synthesis of D-amino acid N-alkylamide catalyzed by D-aminopeptidase
    • Kato Y., Asano Y., Nakazawa A., Kondo K. First stereoselective synthesis of D-amino acid N-alkylamide catalyzed by D-aminopeptidase. Tetrahedron. 45:1989;5743-5754.
    • (1989) Tetrahedron , vol.45 , pp. 5743-5754
    • Kato, Y.1    Asano, Y.2    Nakazawa, A.3    Kondo, K.4
  • 12
    • 0000781832 scopus 로고
    • Synthesis of D-alanine oligopeptides catalyzed by D-aminopeptidase in non-aqueous media
    • Kato Y., Asano Y., Nakazawa A., Kondo K. Synthesis of D-alanine oligopeptides catalyzed by D-aminopeptidase in non-aqueous media. Biocatalysis. 3:1990;207-215.
    • (1990) Biocatalysis , vol.3 , pp. 207-215
    • Kato, Y.1    Asano, Y.2    Nakazawa, A.3    Kondo, K.4
  • 13
    • 0037450059 scopus 로고    scopus 로고
    • Enhancement of the thermostability and catalytic activity of D-stereospecific amino-acid amidase from Ochrobactrum anthropi SV3 by directed evolution
    • Komeda H., Ishikawa N., Asano Y. Enhancement of the thermostability and catalytic activity of D-stereospecific amino-acid amidase from Ochrobactrum anthropi SV3 by directed evolution. J. Mol. Catal. B. 21:2003;283-290.
    • (2003) J. Mol. Catal. B , vol.21 , pp. 283-290
    • Komeda, H.1    Ishikawa, N.2    Asano, Y.3
  • 14
    • 0029818065 scopus 로고    scopus 로고
    • An alkaline D-stereospecific endopeptidase with β-lactamase activity from Bacillus cereus
    • Asano Y., Ito H., Dairi T., Kato Y. An alkaline D-stereospecific endopeptidase with β-lactamase activity from Bacillus cereus. J. Biol. Chem. 271:1996;30256-30262.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30256-30262
    • Asano, Y.1    Ito, H.2    Dairi, T.3    Kato, Y.4
  • 15
    • 0033545553 scopus 로고    scopus 로고
    • Synthesis of D-phenylalanine oligopeptides catalyzed by alakaline D-peptidase from Bacillus cereus DF4-B
    • Komeda H., Asano Y. Synthesis of D-phenylalanine oligopeptides catalyzed by alakaline D-peptidase from Bacillus cereus DF4-B. J. Mol. Catal. B. 6:1999;379-386.
    • (1999) J. Mol. Catal. B , vol.6 , pp. 379-386
    • Komeda, H.1    Asano, Y.2
  • 16
    • 0023129637 scopus 로고
    • Primary structure of the Streptomyces R61 extracellular DD-peptidase. 1. Cloning into Streptomyces lividans and nucleotide sequence of the gene
    • Duez C., Piron-Fraipont C., Joris B., Dusart J., Urdea M.S., Martial J.A., Frère J.M., Ghuysen J.M. Primary structure of the Streptomyces R61 extracellular DD-peptidase. 1. Cloning into Streptomyces lividans and nucleotide sequence of the gene. Eur. J. Biochem. 162:1987;509-518.
    • (1987) Eur. J. Biochem. , vol.162 , pp. 509-518
    • Duez, C.1    Piron-Fraipont, C.2    Joris, B.3    Dusart, J.4    Urdea, M.S.5    Martial, J.A.6    Frère, J.M.7    Ghuysen, J.M.8
  • 17
    • 0032950946 scopus 로고    scopus 로고
    • MIC231, a naturally occurring insertion cassette from Bacillus cereus
    • Chen Y., Braathen P., Léonard C., Mahillon J. MIC231, a naturally occurring insertion cassette from Bacillus cereus. Mol. Microbiol. 32:1999;657-668.
    • (1999) Mol. Microbiol. , vol.32 , pp. 657-668
    • Chen, Y.1    Braathen, P.2    Léonard, C.3    Mahillon, J.4
  • 19
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue H., Nojima H., Okayama H. High efficiency transformation of Escherichia coli with plasmids. Gene. 96:1990;23-28.
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0032961046 scopus 로고    scopus 로고
    • Molecular analysis of tlrB, an antibiotic-resistance gene from tylosin-producing Streptomyces fradiae, and discovery of a novel resistance mechanism
    • Wilson V.T., Cundliffe E. Molecular analysis of tlrB, an antibiotic-resistance gene from tylosin-producing Streptomyces fradiae, and discovery of a novel resistance mechanism. J. Antibiot. 52:1999;288-296.
    • (1999) J. Antibiot. , vol.52 , pp. 288-296
    • Wilson, V.T.1    Cundliffe, E.2
  • 28
    • 0028806595 scopus 로고
    • The refined crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 Å resolution
    • Kelly J.A., Kuzin A.P. The refined crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 Å resolution. J. Mol. Biol. 254:1995;223-236.
    • (1995) J. Mol. Biol. , vol.254 , pp. 223-236
    • Kelly, J.A.1    Kuzin, A.P.2
  • 30
    • 0027984239 scopus 로고
    • IS231A insertion specificity: Consensus sequence and DNA bending at the target site
    • Hallet B., Rezsöhazy R., Mahillon J., Delcour J. IS231A insertion specificity: consensus sequence and DNA bending at the target site. Mol. Microbiol. 14:1994;131-139.
    • (1994) Mol. Microbiol. , vol.14 , pp. 131-139
    • Hallet, B.1    Rezsöhazy, R.2    Mahillon, J.3    Delcour, J.4
  • 31
    • 38249035252 scopus 로고
    • Tandem location of the cellulase genes on the chromosome of Bacillus sp. strain N-4
    • Fukumori F., Ohishi K., Kudo T., Horikoshi K. Tandem location of the cellulase genes on the chromosome of Bacillus sp. strain N-4. FEMS Microbiol. Lett. 48:1987;65-68.
    • (1987) FEMS Microbiol. Lett. , vol.48 , pp. 65-68
    • Fukumori, F.1    Ohishi, K.2    Kudo, T.3    Horikoshi, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.