Characterization of thimet- and neurolysin-like activities in Escherichia coli M 3 A peptidases and description of a specific substrate.
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[1] M. Norman,et al. Endopeptidases 3.4.24.15 and 24.16 in endothelial cells: potential role in vasoactive peptide metabolism. , 2003, American journal of physiology. Heart and circulatory physiology.
[2] R. Hengge-aronis,et al. Recent insights into the general stress response regulatory network in Escherichia coli. , 2002, Journal of molecular microbiology and biotechnology.
[3] L. Juliano,et al. Selective neurotensin-derived internally quenched fluorogenic substrates for neurolysin (EC 3.4.24.16): comparison with thimet oligopeptidase (EC 3.4.24.15) and neprilysin (EC 3.4.24.11). , 2001, Analytical biochemistry.
[4] J. Vohradský,et al. Proteomic analysis of the bacterial cell cycle , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[5] G. Abbenante,et al. Development and characterization of novel potent and stable inhibitors of endopeptidase EC 3.4.24.15. , 2000, The Biochemical journal.
[6] A. Lupas,et al. Structure and mechanism of ATP-dependent proteases. , 1999, Current opinion in chemical biology.
[7] F. Rul,et al. PepS from Streptococcus thermophilus. A new member of the aminopeptidase T family of thermophilic bacteria. , 1999, European journal of biochemistry.
[8] S. Kaminogawa,et al. Cloning of genes of the aminopeptidase T family from Thermus thermophilus HB8 and Bacillus stearothermophilus NCIB8924: apparent similarity to the leucyl aminopeptidase family. , 1997, Bioscience, biotechnology, and biochemistry.
[9] N. W. Davis,et al. The complete genome sequence of Escherichia coli K-12. , 1997, Science.
[10] S. Jacchieri,et al. Structural features that make oligopeptides susceptible substrates for hydrolysis by recombinant thimet oligopeptidase. , 1997, The Biochemical journal.
[11] L. Shapiro,et al. Caulobacter Lon protease has a critical role in cell-cycle control of DNA methylation. , 1996, Genes & development.
[12] A. Ito,et al. Internally quenched fluorogenic protease substrates: Solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs , 1995, Letters in Peptide Science.
[13] B. Henrich,et al. dcp gene of Escherichia coli: cloning, sequencing, transcript mapping, and characterization of the gene product , 1993, Journal of bacteriology.
[14] C. Miller,et al. Escherichia coli prlC encodes an endopeptidase and is homologous to the Salmonella typhimurium opdA gene , 1992, Journal of bacteriology.
[15] C. Miller,et al. Cloning and nucleotide sequence of the Salmonella typhimurium dcp gene encoding dipeptidyl carboxypeptidase , 1992, Journal of bacteriology.
[16] C. Miller,et al. Cloning and nucleotide sequence of opdA, the gene encoding oligopeptidase A in Salmonella typhimurium , 1992, Journal of bacteriology.
[17] M. Müller. Proteolysis in protein import and export: Signal peptide processing in eu-and prokaryotes , 1992, Experientia.
[18] Maurizi Mr,et al. Proteases and protein degradation in Escherichia coli. , 1992 .
[19] F. Checler,et al. Specific inhibition of endopeptidase 24.16 by dipeptides. , 1991, European journal of biochemistry.
[20] T. Yoshimoto,et al. Protease II from Escherichia coli: sequencing and expression of the enzyme gene and characterization of the expressed enzyme. , 1991, Journal of biochemistry.
[21] L. Juliano,et al. Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins. , 1991, Analytical biochemistry.
[22] A. Barrett,et al. The activities of 'Pz-peptidase' and 'endopeptidase 24.15' are due to a single enzyme. , 1989, The Biochemical journal.
[23] A. Barrett,et al. A continuous fluorimetric assay for clostridial collagenase and Pz-peptidase activity. , 1989, The Biochemical journal.
[24] M. Orłowski,et al. Active site directed N-carboxymethyl peptide inhibitors of a soluble metalloendopeptidase from rat brain. , 1984, Biochemistry.
[25] M. M. Bradford. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.
[26] R. Takata,et al. Cloning and sequencing of the Pz-peptidase gene from Bacillus licheniformis N22. , 1999, Journal of bioscience and bioengineering.
[27] S. Gottesman,et al. Proteases and their targets in Escherichia coli. , 1996, Annual review of genetics.
[28] N. Rawlings,et al. [32] Thimet oligopeptidase and oligopeptidase M or neurolysin , 1995 .
[29] C. A. Conlin,et al. [34] Dipeptidyl carboxypeptidase and oligopeptidase A from Escherichia coli and Salmonella typhimurium , 1995 .
[30] T. Yoshimoto,et al. [15] Oligopeptidase B: Protease II from Escherichia coli , 1994 .