메뉴 건너뛰기




Volumn 7, Issue 4, 2012, Pages

Structural and functional characterization of mature forms of metalloprotease E495 from arctic sea-ice bacterium pseudoalteromonas sp. SM495

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CASEIN; METALLOPROTEINASE; METALLOPROTEINASE E495; OLIGOPEPTIDE; PHYCOCYANIN; TYROSINE; UNCLASSIFIED DRUG;

EID: 84859865063     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0035442     Document Type: Article
Times cited : (19)

References (41)
  • 1
    • 11844253939 scopus 로고    scopus 로고
    • Sea ice-an introduction to its physics, chemistry, biology and geology
    • Oxford, Wiley-Blackwell Publishing
    • Thomas DN, Dieckmann GS, (2003) Sea ice-an introduction to its physics, chemistry, biology and geology. Oxford Wiley-Blackwell Publishing.
    • (2003)
    • Thomas, D.N.1    Dieckmann, G.S.2
  • 2
    • 67349202065 scopus 로고    scopus 로고
    • Biogeochemistry and microbial community composition in sea ice and underlying seawater off East Antarctica during early spring
    • Becquevort S, Dumont I, Tison JL, Lannuzel D, Sauvée ML, et al. (2009) Biogeochemistry and microbial community composition in sea ice and underlying seawater off East Antarctica during early spring. Polar Biol 32: 879-895.
    • (2009) Polar Biol , vol.32 , pp. 879-895
    • Becquevort, S.1    Dumont, I.2    Tison, J.L.3    Lannuzel, D.4    Sauvée, M.L.5
  • 3
    • 66149121843 scopus 로고    scopus 로고
    • Cold adaptation of zinc metalloproteases in the thermolysin family from deep sea and arctic sea ice bacteria revealed by catalytic and structural properties and molecular dynamics
    • Xie BB, Bian F, Chen XL, He HL, Guo J, et al. (2009) Cold adaptation of zinc metalloproteases in the thermolysin family from deep sea and arctic sea ice bacteria revealed by catalytic and structural properties and molecular dynamics. J Biol Chem 284: 9257-9269.
    • (2009) J Biol Chem , vol.284 , pp. 9257-9269
    • Xie, B.B.1    Bian, F.2    Chen, X.L.3    He, H.L.4    Guo, J.5
  • 5
    • 34548580171 scopus 로고    scopus 로고
    • Engineering, expression, purification, and production of recombinant thermolysin
    • Inouye K, Kusano M, Hashida Y, Minoda M, Yasukawa K, (2007) Engineering, expression, purification, and production of recombinant thermolysin. Biotechnol Annu Rev 13: 43-64.
    • (2007) Biotechnol Annu Rev , vol.13 , pp. 43-64
    • Inouye, K.1    Kusano, M.2    Hashida, Y.3    Minoda, M.4    Yasukawa, K.5
  • 6
    • 0030058645 scopus 로고    scopus 로고
    • Purification, characterization, and primary structure of Clostridium perfringens lambda-toxin, a thermolysin-like metalloprotease
    • Jin F, Matsushita O, Katayama S, Jin S, Matsushita C, et al. (1996) Purification, characterization, and primary structure of Clostridium perfringens lambda-toxin, a thermolysin-like metalloprotease. Infect Immun 64: 230-237.
    • (1996) Infect Immun , vol.64 , pp. 230-237
    • Jin, F.1    Matsushita, O.2    Katayama, S.3    Jin, S.4    Matsushita, C.5
  • 7
    • 0027533440 scopus 로고
    • Chemical modification of Vibrio vulnificus metalloprotease with activated polyethylene glycol
    • Narukawa H, Miyoshi S, Shinoda S, (1993) Chemical modification of Vibrio vulnificus metalloprotease with activated polyethylene glycol. FEMS Microbiol Lett 108: 43-46.
    • (1993) FEMS Microbiol Lett , vol.108 , pp. 43-46
    • Narukawa, H.1    Miyoshi, S.2    Shinoda, S.3
  • 8
    • 32944466491 scopus 로고    scopus 로고
    • Molecular cloning of the gene encoding Vibrio metalloproteinase vimelysin and isolation of a mutant with high stability in organic solvents
    • Takahashi T, Ng KK, Oyama H, Oda K, (2005) Molecular cloning of the gene encoding Vibrio metalloproteinase vimelysin and isolation of a mutant with high stability in organic solvents. J Biochem 138: 701-710.
    • (2005) J Biochem , vol.138 , pp. 701-710
    • Takahashi, T.1    Ng, K.K.2    Oyama, H.3    Oda, K.4
  • 10
    • 82455199191 scopus 로고    scopus 로고
    • Extracellular metalloproteases from bacteria
    • Wu JW, Chen XL, (2011) Extracellular metalloproteases from bacteria. Appl Microbiol Biotechnol 92: 253-262.
    • (2011) Appl Microbiol Biotechnol , vol.92 , pp. 253-262
    • Wu, J.W.1    Chen, X.L.2
  • 12
    • 0030221745 scopus 로고    scopus 로고
    • Cloning and Sequence Analysis of a Protease-encoding Gene from the Marine Bacterium Alteromonas sp. Strain O-7
    • Tsujbo H, Miyamoto K, Tanaka K, Kaidzu Y, Imada C, et al. (1996) Cloning and Sequence Analysis of a Protease-encoding Gene from the Marine Bacterium Alteromonas sp. Strain O-7. Biosci Biotechnol Biochem 60: 1284-1288.
    • (1996) Biosci Biotechnol Biochem , vol.60 , pp. 1284-1288
    • Tsujbo, H.1    Miyamoto, K.2    Tanaka, K.3    Kaidzu, Y.4    Imada, C.5
  • 13
    • 2942733563 scopus 로고    scopus 로고
    • New knowledge from old: In silico discovery of novel protein domains in Streptomyces coelicolo
    • Yeats C, Bentley S, Bateman A, (2003) New knowledge from old: In silico discovery of novel protein domains in Streptomyces coelicolo. BMC Microbiol 3: 1-20.
    • (2003) BMC Microbiol , vol.3 , pp. 1-20
    • Yeats, C.1    Bentley, S.2    Bateman, A.3
  • 14
    • 70349454241 scopus 로고    scopus 로고
    • Molecular analysis of the gene encoding a cold-adapted halophilic subtilase from deep-sea psychrotolerant bacterium Pseudoalteromonas sp. SM9913: cloning, expression, characterization and function analysis of the C-terminal PPC domains
    • Yan BQ, Chen XL, Hou XY, He HL, Zhou BC, et al. (2009) Molecular analysis of the gene encoding a cold-adapted halophilic subtilase from deep-sea psychrotolerant bacterium Pseudoalteromonas sp. SM9913: cloning, expression, characterization and function analysis of the C-terminal PPC domains. Extremophiles 13: 725-733.
    • (2009) Extremophiles , vol.13 , pp. 725-733
    • Yan, B.Q.1    Chen, X.L.2    Hou, X.Y.3    He, H.L.4    Zhou, B.C.5
  • 15
    • 0004471243 scopus 로고
    • Isolation and biliprotein characterization of phycobilisomes from the thermophilic cyanobacterium Mastigocladus laminosus Cohn
    • Nies M, Wehrmeyer W, (1980) Isolation and biliprotein characterization of phycobilisomes from the thermophilic cyanobacterium Mastigocladus laminosus Cohn. Planta 150: 330-337.
    • (1980) Planta , vol.150 , pp. 330-337
    • Nies, M.1    Wehrmeyer, W.2
  • 16
    • 77349108158 scopus 로고    scopus 로고
    • Efficient separation and purification of allophycocyanin from Spirulina (Arthrospira) platensis
    • Su HN, Xie BB, Chen XL, Wang JX, Zhang XY, et al. (2010) Efficient separation and purification of allophycocyanin from Spirulina (Arthrospira) platensis. J Appl Phycol 22: 65-70.
    • (2010) J Appl Phycol , vol.22 , pp. 65-70
    • Su, H.N.1    Xie, B.B.2    Chen, X.L.3    Wang, J.X.4    Zhang, X.Y.5
  • 17
    • 0142186143 scopus 로고    scopus 로고
    • Taste improvement of refrigerated meat treated with cold-adapted protease
    • He HL, Chen XL, Li JW, Zhang YZ, Gao PJ, (2004) Taste improvement of refrigerated meat treated with cold-adapted protease. Food Chem 84: 307-311.
    • (2004) Food Chem , vol.84 , pp. 307-311
    • He, H.L.1    Chen, X.L.2    Li, J.W.3    Zhang, Y.Z.4    Gao, P.J.5
  • 18
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira PT, (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem 262: 10035-10038.
    • (1987) J Biol Chem , vol.262 , pp. 10035-10038
    • Matsudaira, P.T.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
    • Laemmli UK, (1970) Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 12344288621 scopus 로고    scopus 로고
    • One-step chromatography method for efficient separation and purification of R-phycoerythrin from Polysiphonia urceolata
    • Liu LN, Chen XL, Zhang XY, Zhang YZ, Zhou BC, (2005) One-step chromatography method for efficient separation and purification of R-phycoerythrin from Polysiphonia urceolata. J Biotechnol 116: 91-100.
    • (2005) J Biotechnol , vol.116 , pp. 91-100
    • Liu, L.N.1    Chen, X.L.2    Zhang, X.Y.3    Zhang, Y.Z.4    Zhou, B.C.5
  • 21
    • 0034014874 scopus 로고    scopus 로고
    • Purification and Characterization of an Extracellular Alkaline Serine Protease from Aspergillus terreus (IJIRA 6.2)
    • Chakrabarti SK, Matsumura N, Ranu RS, (2000) Purification and Characterization of an Extracellular Alkaline Serine Protease from Aspergillus terreus (IJIRA 6.2). Curr Microbiol 40: 239-244.
    • (2000) Curr Microbiol , vol.40 , pp. 239-244
    • Chakrabarti, S.K.1    Matsumura, N.2    Ranu, R.S.3
  • 22
    • 0021359251 scopus 로고
    • A modified azoalbumin technique for the assay of proteolytic enzymes for use in blood group serology
    • Phillips PK, Prior D, Dawes B, (1984) A modified azoalbumin technique for the assay of proteolytic enzymes for use in blood group serology. J Clin Pathol 37: 329-331.
    • (1984) J Clin Pathol , vol.37 , pp. 329-331
    • Phillips, P.K.1    Prior, D.2    Dawes, B.3
  • 23
    • 0014936053 scopus 로고
    • Studies on the Bacillus sutilis neutral-protease and Bacillus thermoproteolyticus thermolysin-catalyzed hydrolysis of dipeptide substrates
    • Feder J, Schuck JM, (1970) Studies on the Bacillus sutilis neutral-protease and Bacillus thermoproteolyticus thermolysin-catalyzed hydrolysis of dipeptide substrates. Biochemistry 9: 2784-2791.
    • (1970) Biochemistry , vol.9 , pp. 2784-2791
    • Feder, J.1    Schuck, J.M.2
  • 24
    • 61349193896 scopus 로고    scopus 로고
    • Hydrolysis of insoluble collagen by deseasin MCP-01 from deep-sea Pseudoalteromonas sp. SM9913: collagenolytic characters, collagen-binding ability of C-terminal polycystic kidney disease domain, and implication for its novel role in deep-sea sedimentary particulate organic nitrogen degradation
    • Zhao GY, Chen XL, Zhao HL, Xie BB, Zhou BC, et al. (2008) Hydrolysis of insoluble collagen by deseasin MCP-01 from deep-sea Pseudoalteromonas sp. SM9913: collagenolytic characters, collagen-binding ability of C-terminal polycystic kidney disease domain, and implication for its novel role in deep-sea sedimentary particulate organic nitrogen degradation. J Biol Chem 283: 36100-36107.
    • (2008) J Biol Chem , vol.283 , pp. 36100-36107
    • Zhao, G.Y.1    Chen, X.L.2    Zhao, H.L.3    Xie, B.B.4    Zhou, B.C.5
  • 26
    • 0030767281 scopus 로고    scopus 로고
    • The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21
    • Gary R, Ludwig DL, Cornelius HL, MacInnes MA, Park MS, (1997) The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21. J Biol Chem 272: 24522-24529.
    • (1997) J Biol Chem , vol.272 , pp. 24522-24529
    • Gary, R.1    Ludwig, D.L.2    Cornelius, H.L.3    MacInnes, M.A.4    Park, M.S.5
  • 27
    • 52249089383 scopus 로고    scopus 로고
    • The Relative Binding Affinities of PDZ Partners for CFTR: A Biochemical Basis for Efficient Endocytic Recycling
    • Cushing PR, Fellows A, Villone D, Boisguerin P, Madden DR, (2008) The Relative Binding Affinities of PDZ Partners for CFTR: A Biochemical Basis for Efficient Endocytic Recycling. Biochemistry 47: 10084-10098.
    • (2008) Biochemistry , vol.47 , pp. 10084-10098
    • Cushing, P.R.1    Fellows, A.2    Villone, D.3    Boisguerin, P.4    Madden, D.R.5
  • 28
    • 13444262384 scopus 로고    scopus 로고
    • CDD: a Conserved Domain Database for protein classification
    • Nucleic Acids Res. 33(Database issue)
    • Marchler-Bauer A, Anderson JB, Cherukuri PF, DeWeese-Scott C, Geer LY, et al. (2005) CDD: a Conserved Domain Database for protein classification. Nucleic Acids Res. 33(Database issue) pp. D192-6.
    • (2005)
    • Marchler-Bauer, A.1    Anderson, J.B.2    Cherukuri, P.F.3    DeWeese-Scott, C.4    Geer, L.Y.5
  • 29
    • 0034213559 scopus 로고    scopus 로고
    • Conservation of polar residues as hot spots at protein interfaces
    • Hu Z, Ma B, Wolfson H, Nussinov R, (2000) Conservation of polar residues as hot spots at protein interfaces. Proteins 39: 331-342.
    • (2000) Proteins , vol.39 , pp. 331-342
    • Hu, Z.1    Ma, B.2    Wolfson, H.3    Nussinov, R.4
  • 30
    • 0037102958 scopus 로고    scopus 로고
    • Monte Carlo simulations of the peptide recognition at the consensus binding site of the constant fragment of human immunoglobulin G: the energy landscape analysis of a hot spot at the intermolecular interface
    • Verkhivker GM, Bouzida D, Gehlhaar DK, Rejto PA, Freer ST, et al. (2002) Monte Carlo simulations of the peptide recognition at the consensus binding site of the constant fragment of human immunoglobulin G: the energy landscape analysis of a hot spot at the intermolecular interface. Proteins 48: 539-557.
    • (2002) Proteins , vol.48 , pp. 539-557
    • Verkhivker, G.M.1    Bouzida, D.2    Gehlhaar, D.K.3    Rejto, P.A.4    Freer, S.T.5
  • 31
    • 0036615260 scopus 로고    scopus 로고
    • Cloning and characterization of extracellular metal protease gene of the algicidal marine bacterium Pseudoalteromonas sp. strain A28
    • Lee SO, Kato J, Nakashima K, Kuroda A, Ikeda T, et al. (2002) Cloning and characterization of extracellular metal protease gene of the algicidal marine bacterium Pseudoalteromonas sp. strain A28. Biosci Biotechnol Biochem 66: 1366-1369.
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 1366-1369
    • Lee, S.O.1    Kato, J.2    Nakashima, K.3    Kuroda, A.4    Ikeda, T.5
  • 33
    • 0030704251 scopus 로고    scopus 로고
    • Functional domains of a zinc metalloprotease from Vibrio vulnificus
    • Miyoshi IM, Wakae H, Tomochika KI, Shinoda S, (1997) Functional domains of a zinc metalloprotease from Vibrio vulnificus. J Bacteriol 179: 7606-7609.
    • (1997) J Bacteriol , vol.179 , pp. 7606-7609
    • Miyoshi, I.M.1    Wakae, H.2    Tomochika, K.I.3    Shinoda, S.4
  • 34
    • 36849067496 scopus 로고    scopus 로고
    • Correlation between cellulose binding and activity of cellulose-binding domain mutants of Humicola grisea cellobiohydrolase
    • Takashima S, Ohno M, Hidaka M, Nakamura A, Masaki H, et al. (2007) Correlation between cellulose binding and activity of cellulose-binding domain mutants of Humicola grisea cellobiohydrolase. FEBS Lett 581 (30): 5891-5896.
    • (2007) FEBS Lett , vol.581 , Issue.30 , pp. 5891-5896
    • Takashima, S.1    Ohno, M.2    Hidaka, M.3    Nakamura, A.4    Masaki, H.5
  • 35
    • 34948863874 scopus 로고    scopus 로고
    • The N-terminal propeptide of Vibrio vulnificus Extracellular Metalloprotease is both an Inhibitor of and a Substrate for the Enzyme. J Bacteriol
    • Chang AK, Park JW, Lee EH, Lee JS, (2007) The N-terminal propeptide of Vibrio vulnificus Extracellular Metalloprotease is both an Inhibitor of and a Substrate for the Enzyme. J Bacteriol. 189: 6832-6838.
    • (2007) , vol.189 , pp. 6832-6838
    • Chang, A.K.1    Park, J.W.2    Lee, E.H.3    Lee, J.S.4
  • 36
    • 34447511576 scopus 로고    scopus 로고
    • A novel type of subtilase from the psychrotolerant bacterium Pseudoalteromonas sp. SM9913: catalytic and structural properties of deseasin MCP-01
    • Chen XL, Xie BB, Lu JT, He HL, Zhang YZ, (2007) A novel type of subtilase from the psychrotolerant bacterium Pseudoalteromonas sp. SM9913: catalytic and structural properties of deseasin MCP-01. Microbiology 153: 2116-2125.
    • (2007) Microbiology , vol.153 , pp. 2116-2125
    • Chen, X.L.1    Xie, B.B.2    Lu, J.T.3    He, H.L.4    Zhang, Y.Z.5
  • 37
    • 24044553899 scopus 로고    scopus 로고
    • Role of the N-terminal polycystic kidney disease domainin chitin degradation by chitinase A from a marine bacterium Alteromonas sp. strain O-7
    • Orikoshi H, Nakayama S, Hanato C, Miyamoto K, Tsujibo H, (2005) Role of the N-terminal polycystic kidney disease domainin chitin degradation by chitinase A from a marine bacterium Alteromonas sp. strain O-7. J App Microbio 99: 551-557.
    • (2005) J App Microbio , vol.99 , pp. 551-557
    • Orikoshi, H.1    Nakayama, S.2    Hanato, C.3    Miyamoto, K.4    Tsujibo, H.5
  • 38
    • 0037424755 scopus 로고    scopus 로고
    • A single surface tryptophan in the chitin-binding domain from Bacillus circulans chitinase A1 plays a pivotal role in binding chitin and can be modified to create an elutable affinity tag
    • Ferrandon S, Sterzenbach T, Mersha FB, Xu MQ, (2003) A single surface tryptophan in the chitin-binding domain from Bacillus circulans chitinase A1 plays a pivotal role in binding chitin and can be modified to create an elutable affinity tag. Biochim Biophys Acta 1621: 31-40.
    • (2003) Biochim Biophys Acta , vol.1621 , pp. 31-40
    • Ferrandon, S.1    Sterzenbach, T.2    Mersha, F.B.3    Xu, M.Q.4
  • 39
    • 67650318248 scopus 로고    scopus 로고
    • Energetics of protein hydrogen bonds
    • Pace CN, (2009) Energetics of protein hydrogen bonds. Nat Struct Mol Biol 16: 681-682.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 681-682
    • Pace, C.N.1
  • 40
    • 58549114185 scopus 로고    scopus 로고
    • Identification of direct residue contacts in protein-protein interaction by message passing
    • Weigt M, White RA, Szurmant H, Hoch JA, Hwa T, (2009) Identification of direct residue contacts in protein-protein interaction by message passing. Proc Natl Acad Sci USA 106: 67-72.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 67-72
    • Weigt, M.1    White, R.A.2    Szurmant, H.3    Hoch, J.A.4    Hwa, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.