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Volumn 2, Issue 1, 2009, Pages 1-10

Aspartic proteinases in Antarctic fish

Author keywords

Antarctica; Aspartic proteinase; Cathepsin; Kinetic analysis; Nothepsin; Pepsin

Indexed keywords

BACTERIA (MICROORGANISMS); CHIONODRACO HAMATUS; MAMMALIA; NOTOTHENIOIDEI; TREMATOMUS BERNACCHII;

EID: 67349280308     PISSN: 18747787     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.margen.2009.03.001     Document Type: Review
Times cited : (14)

References (52)
  • 1
    • 0025276666 scopus 로고
    • Revised 2,3, a structure of porcine pepsin: evidence for a flexible subdomain
    • Abad-Zapatero C., Rydel T.J., and Erickson J. Revised 2,3, a structure of porcine pepsin: evidence for a flexible subdomain. Proteins 8 (1990) 62-81
    • (1990) Proteins , vol.8 , pp. 62-81
    • Abad-Zapatero, C.1    Rydel, T.J.2    Erickson, J.3
  • 2
    • 0028135688 scopus 로고
    • Molecular evolution at subzero temperatures: mitochondrial and nuclear phylogenies of fishes from Antarctica (suborder Notothenioidei), and the evolution of antifreeze glycopeptides
    • Bargelloni L., Ritchie P.A., Patarnello T., Battaglia B., Lambert D.M., and Meyer A. Molecular evolution at subzero temperatures: mitochondrial and nuclear phylogenies of fishes from Antarctica (suborder Notothenioidei), and the evolution of antifreeze glycopeptides. Mol. Biol. Evol. 11 (1994) 854-863
    • (1994) Mol. Biol. Evol. , vol.11 , pp. 854-863
    • Bargelloni, L.1    Ritchie, P.A.2    Patarnello, T.3    Battaglia, B.4    Lambert, D.M.5    Meyer, A.6
  • 4
    • 0029129455 scopus 로고
    • Aspartic proteinases (cyprosins) from Cynara cardunculus spp. Flavescens cv. cardoon; purification, characterisation, and tissue-specific expression
    • Brodelius P.E., Cordeiro M.C., and Pais M.S. Aspartic proteinases (cyprosins) from Cynara cardunculus spp. Flavescens cv. cardoon; purification, characterisation, and tissue-specific expression. Adv. Exp. Med. Biol. 362 (1995) 255-266
    • (1995) Adv. Exp. Med. Biol. , vol.362 , pp. 255-266
    • Brodelius, P.E.1    Cordeiro, M.C.2    Pais, M.S.3
  • 5
    • 0030814882 scopus 로고    scopus 로고
    • Molecular characterisation of ovarian cathepsin D in the rainbow trout, Oncorhynchus mykiss
    • Brooks S., Tyler C.R., Carnevali O., Coward K., and Sumpter J.P. Molecular characterisation of ovarian cathepsin D in the rainbow trout, Oncorhynchus mykiss. Gene 201 (1997) 45-54
    • (1997) Gene , vol.201 , pp. 45-54
    • Brooks, S.1    Tyler, C.R.2    Carnevali, O.3    Coward, K.4    Sumpter, J.P.5
  • 6
    • 0032963373 scopus 로고    scopus 로고
    • Cathepsin D from the liver of the antarctic icefish Chionodraco hamatus exhibits unusual activity and stability at high temperatures1
    • Capasso C., Lees W.E., Capasso A., Scudiero R., Carginale V., Kille P., Kay J., and Parisi E. Cathepsin D from the liver of the antarctic icefish Chionodraco hamatus exhibits unusual activity and stability at high temperatures1. Biochim. Biophys. Acta 1431 (1999) 64-73
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 64-73
    • Capasso, C.1    Lees, W.E.2    Capasso, A.3    Scudiero, R.4    Carginale, V.5    Kille, P.6    Kay, J.7    Parisi, E.8
  • 10
    • 0025297753 scopus 로고
    • X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 A resolution
    • Cooper J.B., Khan G., Taylor G., Tickle I.J., and Blundell T.L. X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 A resolution. J. Mol. Biol. 214 (1990) 199-222
    • (1990) J. Mol. Biol. , vol.214 , pp. 199-222
    • Cooper, J.B.1    Khan, G.2    Taylor, G.3    Tickle, I.J.4    Blundell, T.L.5
  • 12
    • 0025290527 scopus 로고
    • The structure and function of the aspartic proteinases
    • Davies D.R. The structure and function of the aspartic proteinases. Annu. Rev. Biophys. Biophys. Chem. 19 (1990) 189-215
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 189-215
    • Davies, D.R.1
  • 13
    • 0024382416 scopus 로고
    • Cleavage of parathyroid hormone in macrophage endosomes illustrates a novel pathway for intracellular processing of proteins
    • Diment S., Martin K.J., and Stahl P.D. Cleavage of parathyroid hormone in macrophage endosomes illustrates a novel pathway for intracellular processing of proteins. J. Biol. Chem. 264 (1989) 13403-13406
    • (1989) J. Biol. Chem. , vol.264 , pp. 13403-13406
    • Diment, S.1    Martin, K.J.2    Stahl, P.D.3
  • 14
    • 0026539468 scopus 로고
    • Yohimbine-induced seizures involve NMDA and GABAergic transmission
    • Dunn R.W., and Corbett R. Yohimbine-induced seizures involve NMDA and GABAergic transmission. Neuropharmacology 31 (1992) 389-395
    • (1992) Neuropharmacology , vol.31 , pp. 389-395
    • Dunn, R.W.1    Corbett, R.2
  • 15
    • 0023190117 scopus 로고
    • The pH dependence of the hydrolysis of chromogenic substrates of the type, Lys-Pro-Xaa-Yaa-Phe-(NO2)Phe-Arg-Leu, by selected aspartic proteinases: evidence for specific interactions in subsites S3 and S2
    • Dunn B.M., Valler M.J., Rolph C.E., Foundling S.I., Jimenez M., and Kay J. The pH dependence of the hydrolysis of chromogenic substrates of the type, Lys-Pro-Xaa-Yaa-Phe-(NO2)Phe-Arg-Leu, by selected aspartic proteinases: evidence for specific interactions in subsites S3 and S2. Biochim. Biophys. Acta 913 (1987) 122-130
    • (1987) Biochim. Biophys. Acta , vol.913 , pp. 122-130
    • Dunn, B.M.1    Valler, M.J.2    Rolph, C.E.3    Foundling, S.I.4    Jimenez, M.5    Kay, J.6
  • 18
    • 0019743933 scopus 로고
    • Gastric proteinases: structure, function, evolution and mechanism of action
    • Foltmann B. Gastric proteinases: structure, function, evolution and mechanism of action. Essays Biochem. 17 (1981) 52-84
    • (1981) Essays Biochem. , vol.17 , pp. 52-84
    • Foltmann, B.1
  • 19
    • 0030879653 scopus 로고    scopus 로고
    • Hemoglobin metabolism in the malaria parasite Plasmodium falciparum
    • Francis S.E., Sullivan Jr. D.J., and Goldberg D.E. Hemoglobin metabolism in the malaria parasite Plasmodium falciparum. Annu. Rev. Microbiol. 51 (1997) 97-123
    • (1997) Annu. Rev. Microbiol. , vol.51 , pp. 97-123
    • Francis, S.E.1    Sullivan Jr., D.J.2    Goldberg, D.E.3
  • 24
    • 0024256915 scopus 로고
    • Aspartic proteinases in fishes and aquatic invertebrates
    • Gildberg A. Aspartic proteinases in fishes and aquatic invertebrates. Comp. Biochem. Physiol. B 91 (1988) 425-435
    • (1988) Comp. Biochem. Physiol. B , vol.91 , pp. 425-435
    • Gildberg, A.1
  • 25
    • 0025298219 scopus 로고
    • Catalytic properties and chemical composition of pepsins from Atlantic cod (Gadus morhua)
    • Gildberg A., Olsen R.L., and Bjarnason J.B. Catalytic properties and chemical composition of pepsins from Atlantic cod (Gadus morhua). Comp. Biochem. Physiol. B 96 (1990) 323-330
    • (1990) Comp. Biochem. Physiol. B , vol.96 , pp. 323-330
    • Gildberg, A.1    Olsen, R.L.2    Bjarnason, J.B.3
  • 26
    • 0028108664 scopus 로고
    • Comparative modelling of barley-grain aspartic proteinase: a structural rationale for observed hydrolytic specificity
    • Guruprasad K., Tormakangas K., Kervinen J., and Blundell T.L. Comparative modelling of barley-grain aspartic proteinase: a structural rationale for observed hydrolytic specificity. FEBS Lett. 352 (1994) 131-136
    • (1994) FEBS Lett. , vol.352 , pp. 131-136
    • Guruprasad, K.1    Tormakangas, K.2    Kervinen, J.3    Blundell, T.L.4
  • 27
    • 0030749449 scopus 로고    scopus 로고
    • Bacterial aspartic proteinases
    • Hill J., and Phylip L.H. Bacterial aspartic proteinases. FEBS Lett. 409 (1997) 357-360
    • (1997) FEBS Lett. , vol.409 , pp. 357-360
    • Hill, J.1    Phylip, L.H.2
  • 29
    • 0031671557 scopus 로고    scopus 로고
    • Tests for ancient species flocks based on molecular phylogenetic appraisals of Sebastes rockfishes and other marine fishes
    • Johns G.C., and Avise J.C. Tests for ancient species flocks based on molecular phylogenetic appraisals of Sebastes rockfishes and other marine fishes. Evolution 52 (1998) 1135-1146
    • (1998) Evolution , vol.52 , pp. 1135-1146
    • Johns, G.C.1    Avise, J.C.2
  • 30
    • 0036181085 scopus 로고    scopus 로고
    • Pepsinogens, progastricsins, and prochymosins: structure, function, evolution, and development
    • Kageyama T. Pepsinogens, progastricsins, and prochymosins: structure, function, evolution, and development. Cell. Mol. Life Sci. 59 (2002) 288-306
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 288-306
    • Kageyama, T.1
  • 31
    • 0024586972 scopus 로고
    • Difference of activation processes and structure of activation peptides in human pepsinogens A and progastricsin
    • Kageyama T., Ichinose M., Miki K., Athauda S.B., Tanji M., and Takahashi K. Difference of activation processes and structure of activation peptides in human pepsinogens A and progastricsin. J. Biochem. (Tokyo) 105 (1989) 15-22
    • (1989) J. Biochem. (Tokyo) , vol.105 , pp. 15-22
    • Kageyama, T.1    Ichinose, M.2    Miki, K.3    Athauda, S.B.4    Tanji, M.5    Takahashi, K.6
  • 33
    • 0024271251 scopus 로고
    • Molecular cloning of multiple bovine aspartyl protease genes
    • Lu Q., Wolfe K.H., and McConnell D.J. Molecular cloning of multiple bovine aspartyl protease genes. Gene 71 (1988) 135-146
    • (1988) Gene , vol.71 , pp. 135-146
    • Lu, Q.1    Wolfe, K.H.2    McConnell, D.J.3
  • 34
    • 0032168540 scopus 로고    scopus 로고
    • New directions in comparative physiology and biochemistry: mechanisms, adaptations, and evolution
    • Mangum C.P., and Hochachka P.W. New directions in comparative physiology and biochemistry: mechanisms, adaptations, and evolution. Physiol. Biochem. Zool. 71 (1998) 471-484
    • (1998) Physiol. Biochem. Zool. , vol.71 , pp. 471-484
    • Mangum, C.P.1    Hochachka, P.W.2
  • 35
    • 0017091634 scopus 로고
    • Mode of inhibition of acid proteases by pepstatin
    • Marciniszyn Jr. J., Hartsuck J.A., and Tang J. Mode of inhibition of acid proteases by pepstatin. J. Biol. Chem. 251 (1976) 7088-7094
    • (1976) J. Biol. Chem. , vol.251 , pp. 7088-7094
    • Marciniszyn Jr., J.1    Hartsuck, J.A.2    Tang, J.3
  • 36
    • 0030749081 scopus 로고    scopus 로고
    • Cold-adapted enzymes
    • Marshall C.J. Cold-adapted enzymes. Trends Biotechnol. 15 (1997) 359-364
    • (1997) Trends Biotechnol. , vol.15 , pp. 359-364
    • Marshall, C.J.1
  • 37
    • 0027414640 scopus 로고
    • Two crystal structures for cathepsin D: the lysosomal targeting signal and active site
    • Metcalf P., and Fusek M. Two crystal structures for cathepsin D: the lysosomal targeting signal and active site. Embo. J. 12 (1993) 1293-1302
    • (1993) Embo. J. , vol.12 , pp. 1293-1302
    • Metcalf, P.1    Fusek, M.2
  • 38
    • 0031415284 scopus 로고    scopus 로고
    • Subtilisin from psychrophilic antarctic bacteria: characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold
    • Narinx E., Baise E., and Gerday C. Subtilisin from psychrophilic antarctic bacteria: characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold. Protein Eng. 10 (1997) 1271-1279
    • (1997) Protein Eng. , vol.10 , pp. 1271-1279
    • Narinx, E.1    Baise, E.2    Gerday, C.3
  • 39
    • 0026620457 scopus 로고
    • Intrinsic activity of precursor forms of HIV-1 proteinase
    • Phylip L.H., Mills J.S., Parten B.F., Dunn B.M., and Kay J. Intrinsic activity of precursor forms of HIV-1 proteinase. FEBS Lett. 314 (1992) 449-454
    • (1992) FEBS Lett. , vol.314 , pp. 449-454
    • Phylip, L.H.1    Mills, J.S.2    Parten, B.F.3    Dunn, B.M.4    Kay, J.5
  • 42
    • 0029094078 scopus 로고
    • Purification and characterization of an acid proteinase from Dirofilaria immitis worms
    • Sato K., Nagai Y., and Suzuki M. Purification and characterization of an acid proteinase from Dirofilaria immitis worms. Adv. Exp. Med. Biol. 362 (1995) 299-304
    • (1995) Adv. Exp. Med. Biol. , vol.362 , pp. 299-304
    • Sato, K.1    Nagai, Y.2    Suzuki, M.3
  • 43
    • 0025354599 scopus 로고
    • Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution
    • Sielecki A.R., Fedorov A.A., Boodhoo A., Andreeva N.S., and James M.N. Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution. J. Mol. Biol. 214 (1990) 143-170
    • (1990) J. Mol. Biol. , vol.214 , pp. 143-170
    • Sielecki, A.R.1    Fedorov, A.A.2    Boodhoo, A.3    Andreeva, N.S.4    James, M.N.5
  • 44
    • 0027214757 scopus 로고
    • Isolation and biochemical characterization of procathepsin E from human erythrocyte membranes
    • Takeda-Ezaki M., and Yamamoto K. Isolation and biochemical characterization of procathepsin E from human erythrocyte membranes. Arch. Biochem. Biophys. 304 (1993) 352-358
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 352-358
    • Takeda-Ezaki, M.1    Yamamoto, K.2
  • 45
    • 85047690480 scopus 로고
    • Tuna pepsinogens and pepsins. Purification, characterization and amino-terminal sequences
    • Tanji M., Kageyama T., and Takahashi K. Tuna pepsinogens and pepsins. Purification, characterization and amino-terminal sequences. Eur. J. Biochem. 177 (1988) 251-259
    • (1988) Eur. J. Biochem. , vol.177 , pp. 251-259
    • Tanji, M.1    Kageyama, T.2    Takahashi, K.3
  • 46
    • 0029002927 scopus 로고
    • A pepstatin-insensitive aspartic proteinase from a thermophilic Bacillus sp
    • Toogood H.S., Prescott M., and Daniel R.M. A pepstatin-insensitive aspartic proteinase from a thermophilic Bacillus sp. Biochem. J. 307 Pt 3 (1995) 783-789
    • (1995) Biochem. J. , vol.307 , Issue.PART 3 , pp. 783-789
    • Toogood, H.S.1    Prescott, M.2    Daniel, R.M.3
  • 47
    • 0028362930 scopus 로고
    • Identification and characterization of lysosomal enzymes involved in the proteolysis of phenobarbital-inducible cytochrome P450
    • Tsuji H., and Akasaki K. Identification and characterization of lysosomal enzymes involved in the proteolysis of phenobarbital-inducible cytochrome P450. Biol. Pharm. Bull. 17 (1994) 568-571
    • (1994) Biol. Pharm. Bull. , vol.17 , pp. 568-571
    • Tsuji, H.1    Akasaki, K.2
  • 48
    • 0024412693 scopus 로고
    • The selectivity of cathepsin D suggests an involvement of the enzyme in the generation of T-cell epitopes
    • van Noort J.M., and van der Drift A.C. The selectivity of cathepsin D suggests an involvement of the enzyme in the generation of T-cell epitopes. J. Biol. Chem. 264 (1989) 14159-14164
    • (1989) J. Biol. Chem. , vol.264 , pp. 14159-14164
    • van Noort, J.M.1    van der Drift, A.C.2
  • 49
    • 0030444391 scopus 로고    scopus 로고
    • Retroviral proteases: structure, function and inhibition from a non-anticipated viral enzyme to the target of a most promising HIV therapy
    • von der Helm K. Retroviral proteases: structure, function and inhibition from a non-anticipated viral enzyme to the target of a most promising HIV therapy. Biol. Chem. 377 (1996) 765-774
    • (1996) Biol. Chem. , vol.377 , pp. 765-774
    • von der Helm, K.1
  • 51
    • 17144458475 scopus 로고    scopus 로고
    • Crystal structure of the aspartic proteinase from Rhizomucor miehei at 2.15 Å resolution
    • Yang J., Teplayakov A., and Quail J.W. Crystal structure of the aspartic proteinase from Rhizomucor miehei at 2.15 Å resolution. J. Mol. Biol. 268 (1997) 449-459
    • (1997) J. Mol. Biol. , vol.268 , pp. 449-459
    • Yang, J.1    Teplayakov, A.2    Quail, J.W.3


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