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Volumn 370, Issue 2, 2003, Pages 567-578

Effect of mutation of two critical glutamic acid residues on the activity and stability of human carboxypeptidase M and characterization of its signal for glycosylphosphatidylinositol anchoring

Author keywords

Membrane anchoring; Peptidase; Peptide metabolism; Recombinant protein expression; Site directed mutagenesis

Indexed keywords

CARBOXYLIC ACIDS; CATALYST ACTIVITY; CONFORMATIONS; ENZYMES; MUTAGENESIS;

EID: 0037335653     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021495     Document Type: Article
Times cited : (20)

References (57)
  • 1
    • 0031886603 scopus 로고    scopus 로고
    • Cellular carboxypeptidases
    • Skidgel, R. A. and Erdös, E. G. (1998) Cellular carboxypeptidases. Immunol. Rev. 161, 129-141
    • (1998) Immunol. Rev. , vol.161 , pp. 129-141
    • Skidgel, R.A.1    Erdös, E.G.2
  • 2
    • 0023690624 scopus 로고
    • Basic carboxypeptidases: Regulators of peptide hormone activity
    • Skidgel, R. A. (1988) Basic carboxypeptidases: regulators of peptide hormone activity. Trends Pharmacol. Sci. 9, 299-304
    • (1988) Trends Pharmacol. Sci. , vol.9 , pp. 299-304
    • Skidgel, R.A.1
  • 3
    • 0021683271 scopus 로고
    • Hydrolysis of opioid hexapeptides by carboxypeptidase N. Presence of carboxypeptidase in cell membranes
    • Skidgel, R. A., Johnson, A. R. and Erdös, E. G. (1984) Hydrolysis of opioid hexapeptides by carboxypeptidase N. Presence of carboxypeptidase in cell membranes. Biochem. Pharmacol. 33, 3471-3478
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 3471-3478
    • Skidgel, R.A.1    Johnson, A.R.2    Erdös, E.G.3
  • 4
    • 0024552834 scopus 로고
    • Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones
    • Skidgel, R. A., Davis, R. M. and Tan, F. (1989) Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones. J. Biol. Chem. 264, 2236-2241
    • (1989) J. Biol. Chem. , vol.264 , pp. 2236-2241
    • Skidgel, R.A.1    Davis, R.M.2    Tan, F.3
  • 5
    • 0026072823 scopus 로고
    • Structure, function and membrane anchoring of carboxypeptidase M
    • Skidgel, R. A., Tan, F., Deddish, P. A. and Li, X. Y. (1991) Structure, function and membrane anchoring of carboxypeptidase M. Biomed. Biochim. Acta 50, 815-820
    • (1991) Biomed. Biochim. Acta , vol.50 , pp. 815-820
    • Skidgel, R.A.1    Tan, F.2    Deddish, P.A.3    Li, X.Y.4
  • 6
    • 0025024253 scopus 로고
    • Carboxypeptidase M in Madin-Darby canine kidney cells. Evidence that carboxypeptidase M has a phosphatidylinositol glycan anchor
    • Deddish, P. A., Skidgel, R. A., Kriho, V. B., Li, X. Y., Becker, R. P. and Erdös, E. G. (1990) Carboxypeptidase M in Madin-Darby canine kidney cells. Evidence that carboxypeptidase M has a phosphatidylinositol glycan anchor. J. Biol. Chem. 265, 15083-15089
    • (1990) J. Biol. Chem. , vol.265 , pp. 15083-15089
    • Deddish, P.A.1    Skidgel, R.A.2    Kriho, V.B.3    Li, X.Y.4    Becker, R.P.5    Erdös, E.G.6
  • 7
    • 0024372894 scopus 로고
    • Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N
    • Tan, F., Chan, S. J., Steiner, D. F., Schilling, J. W. and Skidgel, R. A. (1989) Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N. J. Biol. Chem. 264, 13165-13170
    • (1989) J. Biol. Chem. , vol.264 , pp. 13165-13170
    • Tan, F.1    Chan, S.J.2    Steiner, D.F.3    Schilling, J.W.4    Skidgel, R.A.5
  • 8
    • 0001995439 scopus 로고    scopus 로고
    • Structure and function of mammalian zinc carboxypeptidases
    • Hooper, N. M., ed., Taylor and Francis, London
    • Skidgel, R. A. (1996) Structure and function of mammalian zinc carboxypeptidases. In Zinc Metalloproteases in Health and Disease (Hooper, N. M., ed.), pp. 241-283, Taylor and Francis, London
    • (1996) Zinc Metalloproteases in Health and Disease , pp. 241-283
    • Skidgel, R.A.1
  • 9
    • 0030713420 scopus 로고    scopus 로고
    • Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains
    • Tan, F., Rehli, M., Krause, S. W. and Skidgel, R. A. (1997) Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains. Biochem. J. 327, 81-87
    • (1997) Biochem. J. , vol.327 , pp. 81-87
    • Tan, F.1    Rehli, M.2    Krause, S.W.3    Skidgel, R.A.4
  • 11
    • 0030888061 scopus 로고    scopus 로고
    • Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase
    • Song, L. and Fricker, L. D. (1997) Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase. J. Biol. Chem. 272, 10543-10550
    • (1997) J. Biol. Chem. , vol.272 , pp. 10543-10550
    • Song, L.1    Fricker, L.D.2
  • 12
    • 0031733725 scopus 로고    scopus 로고
    • Identification of mouse CPX-2, a novel member of the metallocarboxypeptidase gene family: cDNA cloning, mRNA distribution, and protein expression and characterization
    • Xin, X., Day, R., Dong, W., Lei, Y. and Fricker, L. D. (1998) Identification of mouse CPX-2, a novel member of the metallocarboxypeptidase gene family: cDNA cloning, mRNA distribution, and protein expression and characterization. DNA Cell Biol. 17, 897-909
    • (1998) DNA Cell Biol. , vol.17 , pp. 897-909
    • Xin, X.1    Day, R.2    Dong, W.3    Lei, Y.4    Fricker, L.D.5
  • 13
    • 0035200832 scopus 로고    scopus 로고
    • Carboxypeptidases from A to Z: Implications in embryonic development and Wnt binding
    • Reznik, S. E. and Fricker, L. D. (2001) Carboxypeptidases from A to Z: implications in embryonic development and Wnt binding. Cell. Mol. Life Sci. 58, 1790-1804
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1790-1804
    • Reznik, S.E.1    Fricker, L.D.2
  • 14
    • 0022519470 scopus 로고
    • Cloning and sequence analysis of cDNA for bovine carboxypeptidase E
    • Fricker, L. D., Evans, C. J., Esch, F. S. and Herbert, E. (1986) Cloning and sequence analysis of cDNA for bovine carboxypeptidase E. Nature (London) 323, 461-464
    • (1986) Nature (London) , vol.323 , pp. 461-464
    • Fricker, L.D.1    Evans, C.J.2    Esch, F.S.3    Herbert, E.4
  • 18
    • 0028111532 scopus 로고
    • Catalytic conformation of carboxypeptidase A. Structure of a true enzyme reaction intermediate determined by electron nuclear double resonance
    • Mustafi, D. and Makinen, M. W. (1994) Catalytic conformation of carboxypeptidase A. Structure of a true enzyme reaction intermediate determined by electron nuclear double resonance. J. Biol. Chem. 269, 4587-4595
    • (1994) J. Biol. Chem. , vol.269 , pp. 4587-4595
    • Mustafi, D.1    Makinen, M.W.2
  • 19
    • 0037177891 scopus 로고    scopus 로고
    • Identification and characterization of three members of the human metallocarboxypeptidase gene family
    • Wei, S., Segura, S., Vendrell, J., Aviles, F. X., Lanoue, E., Day, R., Feng, Y. and Fricker, L. D. (2002) Identification and characterization of three members of the human metallocarboxypeptidase gene family. J. Biol. Chem. 277, 14954-14964
    • (2002) J. Biol. Chem. , vol.277 , pp. 14954-14964
    • Wei, S.1    Segura, S.2    Vendrell, J.3    Aviles, F.X.4    Lanoue, E.5    Day, R.6    Feng, Y.7    Fricker, L.D.8
  • 20
    • 0028862371 scopus 로고
    • A eukaryotic transcriptional repressor with carboxypeptidase activity
    • He, G. P., Mulse, A., Li, A. W. and Ro, H. S. (1995) A eukaryotic transcriptional repressor with carboxypeptidase activity. Nature (London) 378, 92-96
    • (1995) Nature (London) , vol.378 , pp. 92-96
    • He, G.P.1    Mulse, A.2    Li, A.W.3    Ro, H.S.4
  • 21
    • 0033569456 scopus 로고    scopus 로고
    • Enzymic characterization of a novel member of the regulatory B-like carboxypeptidase with transcriptional repression function: Stimulation of enzymic activity by its target DNA
    • Muise, A. M. and Ro, H. S. (1999) Enzymic characterization of a novel member of the regulatory B-like carboxypeptidase with transcriptional repression function: stimulation of enzymic activity by its target DNA. Biochem. J. 343, 341-345
    • (1999) Biochem. J. , vol.343 , pp. 341-345
    • Muise, A.M.1    Ro, H.S.2
  • 22
    • 0037028497 scopus 로고    scopus 로고
    • Structure of the human carboxypeptidase M gene. Identification of a proximal GC-rich promoter and a unique distal promoter that consists of repetitive elements
    • Li, J., Rehli, M., Timblin, B., Tan, F., Krause, S. W. and Skidgel, R. A. (2002) Structure of the human carboxypeptidase M gene. Identification of a proximal GC-rich promoter and a unique distal promoter that consists of repetitive elements. Gene 284, 189-202
    • (2002) Gene , vol.284 , pp. 189-202
    • Li, J.1    Rehli, M.2    Timblin, B.3    Tan, F.4    Krause, S.W.5    Skidgel, R.A.6
  • 25
    • 0017825437 scopus 로고
    • Human plasma carboxypeptidase N. Isolation and characterization
    • Plummer, T. H. J. and Hurwitz, M. Y. (1978) Human plasma carboxypeptidase N. Isolation and characterization. J. Biol. Chem. 253, 3907-3912
    • (1978) J. Biol. Chem. , vol.253 , pp. 3907-3912
    • Plummer, T.H.J.1    Hurwitz, M.Y.2
  • 26
    • 0029060126 scopus 로고
    • Human carboxypeptidase N: Lysine carboxypeptidase
    • Skidgel, R. A. (1995) Human carboxypeptidase N: lysine carboxypeptidase. Methods Enzymol. 248, 653-663
    • (1995) Methods Enzymol. , vol.248 , pp. 653-663
    • Skidgel, R.A.1
  • 27
    • 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. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0017384798 scopus 로고
    • Assay for protein by dye binding
    • van Kley, H. and Hale, S. M. (1977) Assay for protein by dye binding. Anal. Biochem. 81, 485-487
    • (1977) Anal. Biochem. , vol.81 , pp. 485-487
    • Van Kley, H.1    Hale, S.M.2
  • 29
    • 0017366898 scopus 로고
    • An evaluation of the Coomassie brillant blue G-250 dye-binding method for quantitative protein determination
    • Pierce, J. and Suelter, C. H. (1977) An evaluation of the Coomassie brillant blue G-250 dye-binding method for quantitative protein determination. Anal. Biochem. 81, 478-480
    • (1977) Anal. Biochem. , vol.81 , pp. 478-480
    • Pierce, J.1    Suelter, C.H.2
  • 30
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C. and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 31
    • 0025007696 scopus 로고
    • Erratum
    • Erratum (1990) Anal. Biochem. 189, 283
    • (1990) Anal. Biochem. , vol.189 , pp. 283
  • 32
    • 0023654822 scopus 로고
    • Biochemistry of the glycosyl-phosphatidylinositol membrane protein anchors
    • Low, M. G. (1987) Biochemistry of the glycosyl-phosphatidylinositol membrane protein anchors. Biochem. J. 244, 1-13
    • (1987) Biochem. J. , vol.244 , pp. 1-13
    • Low, M.G.1
  • 33
    • 0033614445 scopus 로고    scopus 로고
    • Release of glycosylphosphatidylinositol-anchored carboxypeptidase M by phosphatidylinositol-specific phospholipase C upregulates enzyme synthesis
    • Li, X. Y. and Skidgel, R. A. (1999) Release of glycosylphosphatidylinositol-anchored carboxypeptidase M by phosphatidylinositol-specific phospholipase C upregulates enzyme synthesis. Biochem. Biophys. Res. Commun. 258, 204-210
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 204-210
    • Li, X.Y.1    Skidgel, R.A.2
  • 34
    • 0028981209 scopus 로고
    • How glycosylphosphatidylinositol-anchored membrane proteins are made
    • Udenfriend, S. and Kodukula, K. (1995) How glycosylphosphatidylinositol-anchored membrane proteins are made. Annu. Rev. Biochem. 64, 563-591
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 563-591
    • Udenfriend, S.1    Kodukula, K.2
  • 35
    • 0026780325 scopus 로고
    • Phosphatidylinositol glycan (PI-G) anchored membrane proteins. Amino acid requirements adjacent to the site of cleavage and PI-G attachment in the COOH-terminal signal peptide
    • Gerber, L. D., Kodukula, K. and Udenfriend, S. (1992) Phosphatidylinositol glycan (PI-G) anchored membrane proteins. Amino acid requirements adjacent to the site of cleavage and PI-G attachment in the COOH-terminal signal peptide. J. Biol. Chem. 267, 12168-12173
    • (1992) J. Biol. Chem. , vol.267 , pp. 12168-12173
    • Gerber, L.D.1    Kodukula, K.2    Udenfriend, S.3
  • 36
    • 0025073250 scopus 로고
    • Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase
    • Micanovic, R., Gerber, L. D., Berger, J., Kodukula, K. and Udenfriend, S. (1990) Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase. Proc. Natl. Acad. Sci. U.S.A. 87, 157-161
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 157-161
    • Micanovic, R.1    Gerber, L.D.2    Berger, J.3    Kodukula, K.4    Udenfriend, S.5
  • 37
    • 0032929059 scopus 로고    scopus 로고
    • Optimising the signal peptide for glycosyl phosphatidylinositol modification of human acetylcholinesterase using mutational analysis and peptide-quantitative structure-activity relationships
    • Bucht, G., Wikstrom, P. and Hjalmarsson, K. (1999) Optimising the signal peptide for glycosyl phosphatidylinositol modification of human acetylcholinesterase using mutational analysis and peptide-quantitative structure-activity relationships. Biochim. Biophys. Acta 1431, 471-482
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 471-482
    • Bucht, G.1    Wikstrom, P.2    Hjalmarsson, K.3
  • 38
    • 0026033050 scopus 로고
    • Glycophospholipid membrane anchor attachment. Molecular analysis of the cleavage/attachment site
    • Moran, P., Raab, H., Kohr, W. J. and Caras, I. W. (1991) Glycophospholipid membrane anchor attachment. Molecular analysis of the cleavage/attachment site. J. Biol. Chem. 266, 1250-1257
    • (1991) J. Biol. Chem. , vol.266 , pp. 1250-1257
    • Moran, P.1    Raab, H.2    Kohr, W.J.3    Caras, I.W.4
  • 39
    • 0035958951 scopus 로고    scopus 로고
    • Addition of a glycophosphatidylinositol to acetylcholinesterase. Processing, degradation, and secretion
    • Coussen, F., Ayon, A., Le-Goff, A., Leroy, J., Massoulie, J. and Bon, S. (2001) Addition of a glycophosphatidylinositol to acetylcholinesterase. Processing, degradation, and secretion. J. Biol. Chem. 276, 27881-27892
    • (2001) J. Biol. Chem. , vol.276 , pp. 27881-27892
    • Coussen, F.1    Ayon, A.2    Le-Goff, A.3    Leroy, J.4    Massoulie, J.5    Bon, S.6
  • 40
    • 0026488395 scopus 로고
    • Proteins containing an uncleaved signal for glycophosphatidylinositol membrane anchor attachment are retained in a post-ER compartment
    • Moran, P. and Caras, I. W. (1992) Proteins containing an uncleaved signal for glycophosphatidylinositol membrane anchor attachment are retained in a post-ER compartment. J. Cell Biol. 119, 763-772
    • (1992) J. Cell Biol. , vol.119 , pp. 763-772
    • Moran, P.1    Caras, I.W.2
  • 41
    • 0029037579 scopus 로고
    • Carbonic anhydrase IV: Role of removal of C-terminal domain in glycosylphosphatidylinositol anchoring and realization of enzyme activity
    • Okuyama, T., Waheed, A., Kusumoto, W., Zhu, X. L. and Sly, W. S. (1995) Carbonic anhydrase IV: role of removal of C-terminal domain in glycosylphosphatidylinositol anchoring and realization of enzyme activity. Arch. Biochem. Biophys. 320, 315-322
    • (1995) Arch. Biochem. Biophys. , vol.320 , pp. 315-322
    • Okuyama, T.1    Waheed, A.2    Kusumoto, W.3    Zhu, X.L.4    Sly, W.S.5
  • 42
    • 0027253219 scopus 로고
    • Uncleaved signals for glycosylphosphatidylinositol anchoring cause retention of precursor proteins in the endoplasmic reticulum
    • Delahunty, M. D., Stafford, F. J., Yuan, L. C., Shaz, D. and Bonifacino, J. S. (1993) Uncleaved signals for glycosylphosphatidylinositol anchoring cause retention of precursor proteins in the endoplasmic reticulum. J. Biol. Chem. 268, 12017-12027
    • (1993) J. Biol. Chem. , vol.268 , pp. 12017-12027
    • Delahunty, M.D.1    Stafford, F.J.2    Yuan, L.C.3    Shaz, D.4    Bonifacino, J.S.5
  • 43
    • 0032848027 scopus 로고    scopus 로고
    • Insect cells as hosts for the expression of recombinant glycoproteins
    • Altmann, F., Staudacher, E., Wilson, I. B. and Marz, L. (1999) Insect cells as hosts for the expression of recombinant glycoproteins. Glycoconj. J. 16, 109-123
    • (1999) Glycoconj. J. , vol.16 , pp. 109-123
    • Altmann, F.1    Staudacher, E.2    Wilson, I.B.3    Marz, L.4
  • 44
    • 0024473762 scopus 로고
    • 2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase)
    • 2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase). Biochem. J. 261, 289-291
    • (1989) Biochem. J. , vol.261 , pp. 289-291
    • Deddish, P.A.1    Skidgel, R.A.2    Erdös, E.G.3
  • 45
    • 0034717151 scopus 로고    scopus 로고
    • Replacement of the transmembrane anchor in angiotensin I-converting enzyme (ACE) with a glycosylphosphatidylinositol tail affects activation of the B2 bradykinin receptor by ACE inhibitors
    • Marcic, B., Deddish, P. A., Skidgel, R. A., Erdos, E. G., Minshall, R. D. and Tan, F. (2000) Replacement of the transmembrane anchor in angiotensin I-converting enzyme (ACE) with a glycosylphosphatidylinositol tail affects activation of the B2 bradykinin receptor by ACE inhibitors. J. Biol. Chem. 275, 16110-16118
    • (2000) J. Biol. Chem. , vol.275 , pp. 16110-16118
    • Marcic, B.1    Deddish, P.A.2    Skidgel, R.A.3    Erdos, E.G.4    Minshall, R.D.5    Tan, F.6
  • 46
    • 0023739991 scopus 로고
    • COOH-terminal requirements for the correct processing of a phosphatidylinositol-glycan anchored membrane protein
    • Berger, J., Howard, A. D., Brink, L., Gerber, L., Hauber, J., Cullen, B. R. and Udenfriend, S. (1988) COOH-terminal requirements for the correct processing of a phosphatidylinositol-glycan anchored membrane protein. J. Biol. Chem. 263, 10016-10021
    • (1988) J. Biol. Chem. , vol.263 , pp. 10016-10021
    • Berger, J.1    Howard, A.D.2    Brink, L.3    Gerber, L.4    Hauber, J.5    Cullen, B.R.6    Udenfriend, S.7
  • 47
    • 0025847074 scopus 로고
    • Primary structure and functional activity of a phosphatidylinositol-glycan-specific phospholipase D
    • Scallon, B. J., Fung, W. J., Tsang, T. C., Li, S., Kado-Fong, H., Huang, K. S. and Kochan, J. P. (1991) Primary structure and functional activity of a phosphatidylinositol-glycan-specific phospholipase D. Science 252, 446-448
    • (1991) Science , vol.252 , pp. 446-448
    • Scallon, B.J.1    Fung, W.J.2    Tsang, T.C.3    Li, S.4    Kado-Fong, H.5    Huang, K.S.6    Kochan, J.P.7
  • 48
    • 0026008956 scopus 로고
    • Removal of C6 astrocytoma cell surface molecules with phosphatidylinositol phospholipase C: Effect on regulation of neural cell adhesion molecule isoforms
    • Theveniau, M., Guo, X. J., Rage, P. and Rougon, G. (1991) Removal of C6 astrocytoma cell surface molecules with phosphatidylinositol phospholipase C: effect on regulation of neural cell adhesion molecule isoforms. J. Neurochem. 57, 67-74
    • (1991) J. Neurochem. , vol.57 , pp. 67-74
    • Theveniau, M.1    Guo, X.J.2    Rage, P.3    Rougon, G.4
  • 49
    • 0026022272 scopus 로고
    • Phosphatidylinositol-specific phospholipase C induces biosynthesis of acetylcholinesterase via diacylglycerol in Schistosoma mansoni
    • Espinoza, B., Silman, I., Arnon, R. and Tarrab-Hazdai, R. (1991) Phosphatidylinositol-specific phospholipase C induces biosynthesis of acetylcholinesterase via diacylglycerol in Schistosoma mansoni. Eur. J. Biochem. 195, 863-870
    • (1991) Eur. J. Biochem. , vol.195 , pp. 863-870
    • Espinoza, B.1    Silman, I.2    Arnon, R.3    Tarrab-Hazdai, R.4
  • 50
    • 0026100208 scopus 로고
    • Enhanced secretion from insect cells of a foreign protein fused to the honeybee melittin signal peptide
    • Tessier, D. C., Thomas, D. Y., Khouri, H. E., Laliberté, F. and Vernet, T. (1991) Enhanced secretion from insect cells of a foreign protein fused to the honeybee melittin signal peptide. Gene 98, 177-183
    • (1991) Gene , vol.98 , pp. 177-183
    • Tessier, D.C.1    Thomas, D.Y.2    Khouri, H.E.3    Laliberté, F.4    Vernet, T.5
  • 51
    • 0031439461 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the active site glutamate in human matrilysin: Investigation of its role in catalysis
    • Cha, J. and Auld, D. S. (1997) Site-directed mutagenesis of the active site glutamate in human matrilysin: investigation of its role in catalysis. Biochemistry 36, 16019-16024
    • (1997) Biochemistry , vol.36 , pp. 16019-16024
    • Cha, J.1    Auld, D.S.2
  • 52
    • 0033596982 scopus 로고    scopus 로고
    • Glu300 of rat carboxypeptidase E is essential for enzymatic activity but not substrate binding or routing to the regulated secretory pathway
    • Qian, Y., Varlamov, O. and Fricker, L. D. (1999) Glu300 of rat carboxypeptidase E is essential for enzymatic activity but not substrate binding or routing to the regulated secretory pathway. J. Biol. Chem. 274, 11582-11586
    • (1999) J. Biol. Chem. , vol.274 , pp. 11582-11586
    • Qian, Y.1    Varlamov, O.2    Fricker, L.D.3
  • 53
    • 0242531024 scopus 로고    scopus 로고
    • Crystal structure of avian carboxypeptidase D domain II: A prototype for the regulatory metallocarboxypeptidase subfamily
    • Gomis-Ruth, F. X., Companys, V., Qian, Y., Fricker, L. D., Vendrell, J., Aviles, F. X. and Coll, M. (1999) Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily. EMBO J. 18, 5817-5826
    • (1999) EMBO J. , vol.18 , pp. 5817-5826
    • Gomis-Ruth, F.X.1    Companys, V.2    Qian, Y.3    Fricker, L.D.4    Vendrell, J.5    Aviles, F.X.6    Coll, M.7
  • 54
    • 0035844274 scopus 로고    scopus 로고
    • The crystal structure of the inhibitor-complexed carboxypeptidase D domain II and the modeling of regulatory carboxypeptidases
    • Aloy, P., Companys, V., Vendrell, J., Aviles, F. X., Fricker, L. D., Coll, M. and Gomis-Ruth, F. X. (2001) The crystal structure of the inhibitor-complexed carboxypeptidase D domain II and the modeling of regulatory carboxypeptidases. J. Biol. Chem. 276, 16177-16184
    • (2001) J. Biol. Chem. , vol.276 , pp. 16177-16184
    • Aloy, P.1    Companys, V.2    Vendrell, J.3    Aviles, F.X.4    Fricker, L.D.5    Coll, M.6    Gomis-Ruth, F.X.7
  • 55
    • 15444358269 scopus 로고    scopus 로고
    • Aortic carboxypeptidase-like protein, a novel protein with discoidin and carboxypeptidase-like domains, is up-regulated during vascular smooth muscle cell differentiation
    • Layne, M. D., Endege, W. O., Jain, M. K., Yet, S.-F., Hsieh, C.-M., Chin, M. T., Perrella, M. A., Blanar, M. A., Haber, E. and Lee, M.-E. (1998) Aortic carboxypeptidase-like protein, a novel protein with discoidin and carboxypeptidase-like domains, is up-regulated during vascular smooth muscle cell differentiation. J. Biol. Chem. 273, 15654-15660
    • (1998) J. Biol. Chem. , vol.273 , pp. 15654-15660
    • Layne, M.D.1    Endege, W.O.2    Jain, M.K.3    Yet, S.-F.4    Hsieh, C.-M.5    Chin, M.T.6    Perrella, M.A.7    Blanar, M.A.8    Haber, E.9    Lee, M.-E.10
  • 56
    • 0032478636 scopus 로고    scopus 로고
    • gp180, a protein that binds duck hepatitis B virus particles, has metallocarboxypeptidase D-like enzymatic activity
    • Eng, F. J., Novikova, E. G., Kuroki, K., Ganem, D. and Fricker, L. D. (1998) gp180, a protein that binds duck hepatitis B virus particles, has metallocarboxypeptidase D-like enzymatic activity. J. Biol. Chem. 273, 8382-8388
    • (1998) J. Biol. Chem. , vol.273 , pp. 8382-8388
    • Eng, F.J.1    Novikova, E.G.2    Kuroki, K.3    Ganem, D.4    Fricker, L.D.5
  • 57
    • 0034766658 scopus 로고    scopus 로고
    • A short sequence within domain C of duck carboxypeptidase D is critical for duck hepatitis B virus binding and determines host specificity
    • Spangenberg, H. C., Lee, H. B., Li, J., Tan, F., Skidgel, R., Wands, J. R. and Tong, S. (2001) A short sequence within domain C of duck carboxypeptidase D is critical for duck hepatitis B virus binding and determines host specificity. J. Virol. 75, 10630-10642
    • (2001) J. Virol. , vol.75 , pp. 10630-10642
    • Spangenberg, H.C.1    Lee, H.B.2    Li, J.3    Tan, F.4    Skidgel, R.5    Wands, J.R.6    Tong, S.7


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