메뉴 건너뛰기




Volumn 82, Issue 2, 2014, Pages 300-311

Is the bovine lysosomal phospholipase B-like protein an amidase?

Author keywords

Glycosylation; Lysosomal storage disorders; Ntn hydrolase; Phosphotransferase; X ray structure

Indexed keywords

AMIDASE; AMIDE; BOVINE LYSOSOMAL PHOSPHOLIPASE B LIKE PROTEIN; GLYCAN; HYDROLASE; LYSINE; MANNOSE; N ACETYLGLUCOSAMINE 1 PHOSPHOTRANSFERASE; NUCLEOPHILE; PHOSPHOTRANSFERASE; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 84892680010     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24388     Document Type: Article
Times cited : (13)

References (49)
  • 2
    • 84867616698 scopus 로고    scopus 로고
    • The link between the GBA gene and parkinsonism
    • Sidransky E, Lopez G. The link between the GBA gene and parkinsonism. Lancet Neurol 2012;11:986-998.
    • (2012) Lancet Neurol , vol.11 , pp. 986-998
    • Sidransky, E.1    Lopez, G.2
  • 3
    • 84863482530 scopus 로고    scopus 로고
    • Lysosomal function and dysfunction: mechanism and disease
    • Boya P. Lysosomal function and dysfunction: mechanism and disease. Antioxid Redox Signal 2012;17:766-774.
    • (2012) Antioxid Redox Signal , vol.17 , pp. 766-774
    • Boya, P.1
  • 4
    • 84886482586 scopus 로고    scopus 로고
    • Genetics of lysosomal storage disorders and counselling
    • In: Mehta A, Winchester B, editors. Oxford, UK: John Wiley & Sons, Ltd
    • Hopwood JJ. Genetics of lysosomal storage disorders and counselling. In: Mehta A, Winchester B, editors. Lysosomal storage disorders: a practical guide. Oxford, UK: John Wiley & Sons, Ltd; 2012. pp 29-36.
    • (2012) Lysosomal storage disorders: a practical guide , pp. 29-36
    • Hopwood, J.J.1
  • 5
    • 71049170024 scopus 로고    scopus 로고
    • Mass spectrometry-based protein profiling to determine the cause of lysosomal storage diseases of unknown etiology
    • Zhao C, Wang Y, Xin W, Zheng H, Moore DF, Sims KB
    • Sleat DE, Ding L, Wang S, Zhao C, Wang Y, Xin W, Zheng H, Moore DF, Sims KB. Mass spectrometry-based protein profiling to determine the cause of lysosomal storage diseases of unknown etiology. Mol Cell Proteomics 2009;8:1708-1718.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1708-1718
    • Sleat, D.E.1    Ding, L.2    Wang, S.3
  • 7
    • 57649198155 scopus 로고    scopus 로고
    • The identification of a phospholipase B precursor in human neutrophils
    • Xu S, Zhao L, Larsson A, Venge P. The identification of a phospholipase B precursor in human neutrophils. FEBS J 2009;276:175-186.
    • (2009) FEBS J , vol.276 , pp. 175-186
    • Xu, S.1    Zhao, L.2    Larsson, A.3    Venge, P.4
  • 8
    • 17844387148 scopus 로고    scopus 로고
    • The human brain mannose 6-phosphate glycoproteome: a complex mixture composed of multiple isoforms of many soluble lysosomal proteins
    • Sohar I, Xiao G, Li H, Lobel P
    • Sleat DE, Lackland H, Wang Y, Sohar I, Xiao G, Li H, Lobel P. The human brain mannose 6-phosphate glycoproteome: a complex mixture composed of multiple isoforms of many soluble lysosomal proteins. Proteomics 2005;5:1520-1532.
    • (2005) Proteomics , vol.5 , pp. 1520-1532
    • Sleat, D.E.1    Lackland, H.2    Wang, Y.3
  • 10
    • 79953318188 scopus 로고    scopus 로고
    • Classification of subcellular location by comparative proteomic analysis of native and density-shifted lysosomes
    • Della Valle MC, Sleat DE, Zheng H, Moore DF, Jadot M, Lobel P. Classification of subcellular location by comparative proteomic analysis of native and density-shifted lysosomes. Mol Cell Proteomics 2011;10:M110 006403.
    • (2011) Mol Cell Proteomics , vol.10
    • Della Valle, M.C.1    Sleat, D.E.2    Zheng, H.3    Moore, D.F.4    Jadot, M.5    Lobel, P.6
  • 11
    • 61849164561 scopus 로고    scopus 로고
    • Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry
    • Han G, Wang F, Ye M, Wang L, Zou H.
    • Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H. Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res 2009;8:651-661.
    • (2009) J Proteome Res , vol.8 , pp. 651-661
    • Chen, R.1    Jiang, X.2    Sun, D.3
  • 12
    • 33645723014 scopus 로고    scopus 로고
    • Identification of sites of mannose 6-phosphorylation on lysosomal proteins
    • Sleat DE, Zheng H, Qian M, Lobel P. Identification of sites of mannose 6-phosphorylation on lysosomal proteins. Mol Cell Proteomics 2006;5:686-701.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 686-701
    • Sleat, D.E.1    Zheng, H.2    Qian, M.3    Lobel, P.4
  • 13
    • 33749322938 scopus 로고    scopus 로고
    • Molecular characterization of the hypothetical 66.3-kDa protein in mouse: lysosomal targeting, glycosylation, processing and tissue distribution
    • Deuschl F, Kollmann K, von Figura K, Lubke T. Molecular characterization of the hypothetical 66.3-kDa protein in mouse: lysosomal targeting, glycosylation, processing and tissue distribution. FEBS Lett 2006;580:5747-5752.
    • (2006) FEBS Lett , vol.580 , pp. 5747-5752
    • Deuschl, F.1    Kollmann, K.2    von Figura, K.3    Lubke, T.4
  • 14
    • 33947229039 scopus 로고    scopus 로고
    • Biochemical characterization and lysosomal localization of the mannose-6-phosphate protein p76 (hypothetical protein LOC196463)
    • Jensen AG, Chemali M, Chapel A, Kieffer-Jaquinod S, Jadot M, Garin J, Journet A. Biochemical characterization and lysosomal localization of the mannose-6-phosphate protein p76 (hypothetical protein LOC196463). Biochem J 2007;402:449-458.
    • (2007) Biochem J , vol.402 , pp. 449-458
    • Jensen, A.G.1    Chemali, M.2    Chapel, A.3    Kieffer-Jaquinod, S.4    Jadot, M.5    Garin, J.6    Journet, A.7
  • 15
    • 4544330114 scopus 로고    scopus 로고
    • Identification of phospholipase B from Dictyostelium discoideum reveals a new lipase family present in mammals, flies and nematodes, but not yeast
    • Morgan CP, Insall R, Haynes L, Cockcroft S. Identification of phospholipase B from Dictyostelium discoideum reveals a new lipase family present in mammals, flies and nematodes, but not yeast. Biochem J 2004;382:441-449.
    • (2004) Biochem J , vol.382 , pp. 441-449
    • Morgan, C.P.1    Insall, R.2    Haynes, L.3    Cockcroft, S.4
  • 18
    • 0026540411 scopus 로고
    • The alpha/beta hydrolase fold
    • Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, Sussman JL, Verschueren KHG, Goldman A.
    • Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, Sussman JL, Verschueren KHG, Goldman A. The alpha/beta hydrolase fold. Protein Eng 1992;5:197-211.
    • (1992) Protein Eng , vol.5 , pp. 197-211
    • Ollis, D.L.1    Cheah, E.2    Cygler, M.3
  • 19
    • 0033153557 scopus 로고    scopus 로고
    • Of barn owls and bankers: a lush variety of alpha/beta hydrolases
    • Heikinheimo P, Goldman A, Jeffries C, Ollis DL. Of barn owls and bankers: a lush variety of alpha/beta hydrolases. Structure 1999;7:R141-R146.
    • (1999) Structure , vol.7
    • Heikinheimo, P.1    Goldman, A.2    Jeffries, C.3    Ollis, D.L.4
  • 20
    • 77649140338 scopus 로고    scopus 로고
    • Structures of an isopenicillin N converting Ntn-hydrolase reveal different catalytic roles for the active site residues of precursor and mature enzyme
    • Bokhove M, Yoshida H, Hensgens CM, van der Laan JM, Sutherland JD, Dijkstra BW. Structures of an isopenicillin N converting Ntn-hydrolase reveal different catalytic roles for the active site residues of precursor and mature enzyme. Structure 2010;18:301-308.
    • (2010) Structure , vol.18 , pp. 301-308
    • Bokhove, M.1    Yoshida, H.2    Hensgens, C.M.3    van der Laan, J.M.4    Sutherland, J.D.5    Dijkstra, B.W.6
  • 21
    • 0034495297 scopus 로고    scopus 로고
    • Structural comparison of Ntn-hydrolases
    • Oinonen C, Rouvinen J. Structural comparison of Ntn-hydrolases. Protein Sci 2000;9:2329-2337.
    • (2000) Protein Sci , vol.9 , pp. 2329-2337
    • Oinonen, C.1    Rouvinen, J.2
  • 22
    • 0030921264 scopus 로고    scopus 로고
    • Purification of bovine lysosomal alpha-mannosidase, characterization of its gene and determination of two mutations that cause alpha-mannosidosis
    • Tollersrud OK, Berg T, Healy P, Evjen G, Ramachandran U, Nilssen O. Purification of bovine lysosomal alpha-mannosidase, characterization of its gene and determination of two mutations that cause alpha-mannosidosis. Eur J Biochem 1997;246:410-419.
    • (1997) Eur J Biochem , vol.246 , pp. 410-419
    • Tollersrud, O.K.1    Berg, T.2    Healy, P.3    Evjen, G.4    Ramachandran, U.5    Nilssen, O.6
  • 23
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen FH, Berglund H, Vedadi M. The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat Protoc 2007;2:2212-2221.
    • (2007) Nat Protoc , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 25
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A, Teplyakov A. MOLREP: an automated program for molecular replacement. J Appl Crystallogr 1997;30:1022-1025.
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 26
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Dodson EJ, Emsley P, Evans PR, Keegan RM, Krissinel EB, Leslie AG, McCoy A, McNicholas SJ, Murshudov GN, Pannu NS, Potterton EA, Powell HR, Read RJ, Vagin A, Wilson KS.
    • Winn MD, Ballard CC, Cowtan KD, Dodson EJ, Emsley P, Evans PR, Keegan RM, Krissinel EB, Leslie AG, McCoy A, McNicholas SJ, Murshudov GN, Pannu NS, Potterton EA, Powell HR, Read RJ, Vagin A, Wilson KS. Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 2011;67:235-242.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 235-242
    • Winn, M.D.1    Ballard, C.C.2    Cowtan, K.D.3
  • 27
    • 43749083257 scopus 로고    scopus 로고
    • a program for mutating PDB files used as templates in molecular replacement
    • Stein N. CHAINSAW: a program for mutating PDB files used as templates in molecular replacement. J Appl Crystallogr 2008;41:641-643.
    • (2008) J Appl Crystallogr , vol.41 , pp. 641-643
    • Stein, N.C.1
  • 28
    • 0026597444 scopus 로고
    • Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger AT. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 1992;355:472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 30
  • 32
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: all-atom structure validation for macromolecular crystallography
    • Chen VB, Arendall WB 3rd, Headd JJ, Keedy DA, Immormino RM, Kapral GJ, Murray LW, Richardson JS, Richardson DC.
    • Chen VB, Arendall WBr, Headd JJ, Chen VB, Arendall WB 3rd, Headd JJ, Keedy DA, Immormino RM, Kapral GJ, Murray LW, Richardson JS, Richardson DC. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 2010;66:12-21.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 12-21
    • Chen, V.B.1    Arendall, WB.2    Headd, J.J.3
  • 33
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L, Rosenstrom P. Dali server: conservation mapping in 3D. Nucleic Acids Res 2010;38:W545-W549.
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 34
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K. Inference of macromolecular assemblies from crystalline state. J Mol Biol 2007;372:774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 35
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
    • Gibson TJ, Karplus K, Li W, Lopez R, McWilliam H, Remmert M, Soding J, Thompson JD, Higgins DG.
    • Sievers F, Wilm A, Dineen D, Gibson TJ, Karplus K, Li W, Lopez R, McWilliam H, Remmert M, Soding J, Thompson JD, Higgins DG. Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol Syst Biol 2011;7:539.
    • (2011) Mol Syst Biol , vol.7 , pp. 539
    • Sievers, F.1    Wilm, A.2    Dineen, D.3
  • 36
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy H, Erez E, Martz E, Pupko T, Ben-Tal N. ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res 2010;38:W529-W533.
    • (2010) Nucleic Acids Res , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 38
    • 7444225775 scopus 로고    scopus 로고
    • Novel buffer systems for macromolecular crystallization
    • Newman J. Novel buffer systems for macromolecular crystallization. Acta Crystallogr D Biol Crystallogr 2004;60:610-612.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 610-612
    • Newman, J.1
  • 39
    • 84864366272 scopus 로고    scopus 로고
    • The structure and catalytic cycle of a sodium-pumping pyrophosphatase
    • Kellosalo J, Kajander T, Kogan K, Pokharel K, Goldman A. The structure and catalytic cycle of a sodium-pumping pyrophosphatase. Science 2012;337:473-476.
    • (2012) Science , vol.337 , pp. 473-476
    • Kellosalo, J.1    Kajander, T.2    Kogan, K.3    Pokharel, K.4    Goldman, A.5
  • 40
    • 0028786346 scopus 로고
    • Three-dimensional structure of human lysosomal aspartylglucosaminidase
    • Oinonen C, Tikkanen R, Rouvinen J, Peltonen L. Three-dimensional structure of human lysosomal aspartylglucosaminidase. Nat Struct Biol 1995;2:1102-1108.
    • (1995) Nat Struct Biol , vol.2 , pp. 1102-1108
    • Oinonen, C.1    Tikkanen, R.2    Rouvinen, J.3    Peltonen, L.4
  • 41
    • 0032516825 scopus 로고    scopus 로고
    • Lysine-based structure responsible for selective mannose phosphorylation of cathepsin D and cathepsin L defines a common structural motif for lysosomal enzyme targeting
    • Cuozzo JW, Tao K, Cygler M, Mort JS, Sahagian GG. Lysine-based structure responsible for selective mannose phosphorylation of cathepsin D and cathepsin L defines a common structural motif for lysosomal enzyme targeting. J Biol Chem 1998;273:21067-21076.
    • (1998) J Biol Chem , vol.273 , pp. 21067-21076
    • Cuozzo, J.W.1    Tao, K.2    Cygler, M.3    Mort, J.S.4    Sahagian, G.G.5
  • 42
    • 25844478020 scopus 로고    scopus 로고
    • Identification of the minimal lysosomal enzyme recognition domain in cathepsin D
    • Steet R, Lee WS, Kornfeld S. Identification of the minimal lysosomal enzyme recognition domain in cathepsin D. J Biol Chem 2005;280:33318-33323.
    • (2005) J Biol Chem , vol.280 , pp. 33318-33323
    • Steet, R.1    Lee, W.S.2    Kornfeld, S.3
  • 43
    • 0030780140 scopus 로고    scopus 로고
    • Several cooperating binding sites mediate the interaction of a lysosomal enzyme with phosphotransferase
    • Tikkanen R, Peltola M, Oinonen C, Rouvinen J, Peltonen L. Several cooperating binding sites mediate the interaction of a lysosomal enzyme with phosphotransferase. EMBO J 1997;16:6684-6693.
    • (1997) EMBO J , vol.16 , pp. 6684-6693
    • Tikkanen, R.1    Peltola, M.2    Oinonen, C.3    Rouvinen, J.4    Peltonen, L.5
  • 44
    • 0036830569 scopus 로고    scopus 로고
    • Role of N-linked oligosaccharide flexibility in mannose phosphorylation of lysosomal enzyme cathepsin L
    • Warner JB, Thalhauser C, Tao K, Sahagian GG. Role of N-linked oligosaccharide flexibility in mannose phosphorylation of lysosomal enzyme cathepsin L. J Biol Chem 2002;277:41897-41905.
    • (2002) J Biol Chem , vol.277 , pp. 41897-41905
    • Warner, J.B.1    Thalhauser, C.2    Tao, K.3    Sahagian, G.G.4
  • 45
    • 54349091030 scopus 로고    scopus 로고
    • Protein co-evolution, co-adaptation and interactions
    • Pazos F, Valencia A. Protein co-evolution, co-adaptation and interactions. EMBO J 2008;27:2648-2655.
    • (2008) EMBO J , vol.27 , pp. 2648-2655
    • Pazos, F.1    Valencia, A.2
  • 46
    • 0033615737 scopus 로고    scopus 로고
    • On the diversity of secreted phospholipases A(2). Cloning, tissue distribution, and functional expression of two novel mouse group II enzymes
    • Valentin E, Ghomashchi F, Gelb MH, Lazdunski M, Lambeau G. On the diversity of secreted phospholipases A(2). Cloning, tissue distribution, and functional expression of two novel mouse group II enzymes. J Biol Chem 1999;274:31195-31202.
    • (1999) J Biol Chem , vol.274 , pp. 31195-31202
    • Valentin, E.1    Ghomashchi, F.2    Gelb, M.H.3    Lazdunski, M.4    Lambeau, G.5
  • 47
    • 84867583031 scopus 로고    scopus 로고
    • The structure of human GALNS reveals the molecular basis for mucopolysaccharidosis IV A
    • Rivera-Colon Y, Schutsky EK, Kita AZ, Garman SC. The structure of human GALNS reveals the molecular basis for mucopolysaccharidosis IV A. J Mol Biol 2012;423:736-751.
    • (2012) J Mol Biol , vol.423 , pp. 736-751
    • Rivera-Colon, Y.1    Schutsky, E.K.2    Kita, A.Z.3    Garman, S.C.4
  • 48
    • 84863639111 scopus 로고    scopus 로고
    • Resolving the ortholog conjecture: orthologs tend to be weakly, but significantly, more similar in function than paralogs
    • Altenhoff AM, Studer RA, Robinson-Rechavi M, Dessimoz C. Resolving the ortholog conjecture: orthologs tend to be weakly, but significantly, more similar in function than paralogs. PLoS Comput Biol 2012;8:e1002514.
    • (2012) PLoS Comput Biol , vol.8
    • Altenhoff, A.M.1    Studer, R.A.2    Robinson-Rechavi, M.3    Dessimoz, C.4
  • 49
    • 0017493504 scopus 로고
    • Efficiency and evolution of enzyme catalysis
    • Albery WJ, Knowles JR. Efficiency and evolution of enzyme catalysis. Angew Chem Int Ed Engl 1977;16:285-293.
    • (1977) Angew Chem Int Ed Engl , vol.16 , pp. 285-293
    • Albery, W.J.1    Knowles, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.