메뉴 건너뛰기




Volumn 392, Issue 2, 2009, Pages 393-404

The Structural Basis of β-Peptide-Specific Cleavage by the Serine Protease Cyanophycinase

Author keywords

cyanophycin; cyanophycinase; serine protease; x ray crystal structure; peptide

Indexed keywords

ARGININE; ASPARTIC ACID; CYANOPHYCIN; CYANOPHYCINASE; DIPEPTIDASE; FRESH WATER; GLYCINE; NITROGEN; SERINE; SERINE PROTEINASE; UNCLASSIFIED DRUG;

EID: 68949200799     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.07.001     Document Type: Article
Times cited : (16)

References (50)
  • 1
    • 0025054141 scopus 로고
    • Transient accumulation of cyanophycin in Anabaena cylindrica and Synechocystis 6308
    • Mackerras A.H., DeChazal N.M., and Smith G.D. Transient accumulation of cyanophycin in Anabaena cylindrica and Synechocystis 6308. J. Gen. Microbiol. 136 (1990) 2057-2065
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 2057-2065
    • Mackerras, A.H.1    DeChazal, N.M.2    Smith, G.D.3
  • 2
    • 34447331068 scopus 로고    scopus 로고
    • Analysis of genome sequences for genes of cyanophycin metabolism: identifying putative cyanophycin metabolizing prokaryotes
    • Fuser G., and Steinbuchel A. Analysis of genome sequences for genes of cyanophycin metabolism: identifying putative cyanophycin metabolizing prokaryotes. Macromol. Biosci. 7 (2007) 278-296
    • (2007) Macromol. Biosci. , vol.7 , pp. 278-296
    • Fuser, G.1    Steinbuchel, A.2
  • 3
    • 0016881981 scopus 로고
    • Determination of the structure of the novel polypeptide containing aspartic acid and arginine which is found in Cyanobacteria
    • Simon R.D., and Weathers P. Determination of the structure of the novel polypeptide containing aspartic acid and arginine which is found in Cyanobacteria. Biochim. Biophys. Acta 420 (1976) 165-176
    • (1976) Biochim. Biophys. Acta , vol.420 , pp. 165-176
    • Simon, R.D.1    Weathers, P.2
  • 4
    • 65549102552 scopus 로고    scopus 로고
    • Fixation and fate of C and N in the cyanobacterium Trichodesmium using nanometer-scale secondary ion mass spectrometry
    • Finzi-Hart J.A., Pett-Ridge J., Weber P.K., Popa R., Fallon S.J., Gunderson T., et al. Fixation and fate of C and N in the cyanobacterium Trichodesmium using nanometer-scale secondary ion mass spectrometry. Proc. Natl Acad. Sci. USA 106 (2009) 6345-6350
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 6345-6350
    • Finzi-Hart, J.A.1    Pett-Ridge, J.2    Weber, P.K.3    Popa, R.4    Fallon, S.J.5    Gunderson, T.6
  • 6
    • 54349098431 scopus 로고    scopus 로고
    • A cyanophycin synthetase from Thermosynechococcus elongatus BP-1 catalyzes primer-independent cyanophycin synthesis
    • Arai T., and Kino K. A cyanophycin synthetase from Thermosynechococcus elongatus BP-1 catalyzes primer-independent cyanophycin synthesis. Appl. Microbiol. Biotechnol. 81 (2008) 69-78
    • (2008) Appl. Microbiol. Biotechnol. , vol.81 , pp. 69-78
    • Arai, T.1    Kino, K.2
  • 7
    • 0033850973 scopus 로고    scopus 로고
    • Biosynthesis of the cyanobacterial reserve polymer multi-l-arginyl-poly-l-aspartic acid (cyanophycin): mechanism of the cyanophycin synthetase reaction studied with synthetic primers
    • Berg H., Ziegler K., Piotukh K., Baier K., Lockau W., and Volkmer-Engert R. Biosynthesis of the cyanobacterial reserve polymer multi-l-arginyl-poly-l-aspartic acid (cyanophycin): mechanism of the cyanophycin synthetase reaction studied with synthetic primers. Eur. J. Biochem. 267 (2000) 5561-5570
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5561-5570
    • Berg, H.1    Ziegler, K.2    Piotukh, K.3    Baier, K.4    Lockau, W.5    Volkmer-Engert, R.6
  • 8
    • 0000739749 scopus 로고
    • Cyanophycin granules from the blue-green alga Anabaena cylindrica: a reserve material consisting of copolymers of aspartic acid and arginine
    • Simon R.D. Cyanophycin granules from the blue-green alga Anabaena cylindrica: a reserve material consisting of copolymers of aspartic acid and arginine. Proc. Natl Acad. Sci. USA 68 (1971) 265-267
    • (1971) Proc. Natl Acad. Sci. USA , vol.68 , pp. 265-267
    • Simon, R.D.1
  • 9
    • 0019327321 scopus 로고
    • Structural characterization of the cyanophycin granule polypeptide of Anabaena cylindrica by circular dichroism and Raman spectroscopy
    • Simon R.D., Lawry N.H., and McLendon G.L. Structural characterization of the cyanophycin granule polypeptide of Anabaena cylindrica by circular dichroism and Raman spectroscopy. Biochim. Biophys. Acta 626 (1980) 277-281
    • (1980) Biochim. Biophys. Acta , vol.626 , pp. 277-281
    • Simon, R.D.1    Lawry, N.H.2    McLendon, G.L.3
  • 10
    • 0033064557 scopus 로고    scopus 로고
    • 15N isotopic enrichment of cyanophycin synthesized by the cyanobacterium Synechocystis sp. strain PCC 6308
    • 15N isotopic enrichment of cyanophycin synthesized by the cyanobacterium Synechocystis sp. strain PCC 6308. Biochim. Biophys. Acta 1426 (1999) 429-438
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 429-438
    • Suarez, C.1    Kohler, S.J.2    Allen, M.M.3    Kolodny, N.H.4
  • 11
    • 35649003888 scopus 로고    scopus 로고
    • Assessment of technological options and economical feasibility for cyanophycin biopolymer and high-value amino acid production
    • Mooibroek H., Oosterhuis N., Giuseppin M., Toonen M., Franssen H., Scott E., et al. Assessment of technological options and economical feasibility for cyanophycin biopolymer and high-value amino acid production. Appl. Microbiol. Biotechnol. 77 (2007) 257-267
    • (2007) Appl. Microbiol. Biotechnol. , vol.77 , pp. 257-267
    • Mooibroek, H.1    Oosterhuis, N.2    Giuseppin, M.3    Toonen, M.4    Franssen, H.5    Scott, E.6
  • 12
    • 0036304471 scopus 로고    scopus 로고
    • Technical-scale production of cyanophycin with recombinant strains of Escherichia coli
    • Frey K.M., Oppermann-Sanio F.B., Schmidt H., and Steinbuchel A. Technical-scale production of cyanophycin with recombinant strains of Escherichia coli. Appl. Environ. Microbiol. 68 (2002) 3377-3384
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3377-3384
    • Frey, K.M.1    Oppermann-Sanio, F.B.2    Schmidt, H.3    Steinbuchel, A.4
  • 13
    • 41749088239 scopus 로고    scopus 로고
    • Plastid targeting strategies for cyanophycin synthetase to achieve high-level polymer accumulation in Nicotiana tabacum
    • Huhns M., Neumann K., Hausmann T., Ziegler K., Klemke F., Kahmann U., et al. Plastid targeting strategies for cyanophycin synthetase to achieve high-level polymer accumulation in Nicotiana tabacum. Plant Biotechnol. J. 6 (2008) 321-336
    • (2008) Plant Biotechnol. J. , vol.6 , pp. 321-336
    • Huhns, M.1    Neumann, K.2    Hausmann, T.3    Ziegler, K.4    Klemke, F.5    Kahmann, U.6
  • 14
    • 0033994940 scopus 로고    scopus 로고
    • Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase
    • Lassy R.A., and Miller C.G. Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase. J. Bacteriol. 182 (2000) 2536-2543
    • (2000) J. Bacteriol. , vol.182 , pp. 2536-2543
    • Lassy, R.A.1    Miller, C.G.2
  • 15
    • 0034687682 scopus 로고    scopus 로고
    • The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad
    • Hakansson K., Wang A.H., and Miller C.G. The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad. Proc. Natl Acad. Sci. USA 97 (2000) 14097-14102
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 14097-14102
    • Hakansson, K.1    Wang, A.H.2    Miller, C.G.3
  • 16
    • 0033167939 scopus 로고    scopus 로고
    • Cyanophycinase, a peptidase degrading the cyanobacterial reserve material multi-l-arginyl-poly-l-aspartic acid (cyanophycin): molecular cloning of the gene of Synechocystis sp. PCC 6803, expression in Escherichia coli, and biochemical characterization of the purified enzyme
    • Richter R., Hejazi M., Kraft R., Ziegler K., and Lockau W. Cyanophycinase, a peptidase degrading the cyanobacterial reserve material multi-l-arginyl-poly-l-aspartic acid (cyanophycin): molecular cloning of the gene of Synechocystis sp. PCC 6803, expression in Escherichia coli, and biochemical characterization of the purified enzyme. Eur. J. Biochem. 263 (1999) 163-169
    • (1999) Eur. J. Biochem. , vol.263 , pp. 163-169
    • Richter, R.1    Hejazi, M.2    Kraft, R.3    Ziegler, K.4    Lockau, W.5
  • 17
    • 0842323017 scopus 로고    scopus 로고
    • Isolation and characterization of Gram-positive cyanophycin-degrading bacteria-kinetic studies on cyanophycin depolymerase activity in aerobic bacteria
    • Obst M., Sallam A., Luftmann H., and Steinbuchel A. Isolation and characterization of Gram-positive cyanophycin-degrading bacteria-kinetic studies on cyanophycin depolymerase activity in aerobic bacteria. Biomacromolecules 5 (2004) 153-161
    • (2004) Biomacromolecules , vol.5 , pp. 153-161
    • Obst, M.1    Sallam, A.2    Luftmann, H.3    Steinbuchel, A.4
  • 18
    • 22144476898 scopus 로고    scopus 로고
    • Degradation of cyanophycin by Sedimentibacter hongkongensis strain KI and Citrobacter amalonaticus strain G isolated from an anaerobic bacterial consortium
    • Obst M., Krug A., Luftmann H., and Steinbuchel A. Degradation of cyanophycin by Sedimentibacter hongkongensis strain KI and Citrobacter amalonaticus strain G isolated from an anaerobic bacterial consortium. Appl. Environ. Microbiol. 71 (2005) 3642-3652
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 3642-3652
    • Obst, M.1    Krug, A.2    Luftmann, H.3    Steinbuchel, A.4
  • 19
    • 0037067662 scopus 로고    scopus 로고
    • Isolation of cyanophycin-degrading bacteria, cloning and characterization of an extracellular cyanophycinase gene (cphE) from Pseudomonas anguilliseptica strain BI. The cphE gene from P. anguilliseptica BI encodes a cyanophycin-hydrolyzing enzyme
    • Obst M., Oppermann-Sanio F.B., Luftmann H., and Steinbuchel A. Isolation of cyanophycin-degrading bacteria, cloning and characterization of an extracellular cyanophycinase gene (cphE) from Pseudomonas anguilliseptica strain BI. The cphE gene from P. anguilliseptica BI encodes a cyanophycin-hydrolyzing enzyme. J. Biol. Chem. 277 (2002) 25096-25105
    • (2002) J. Biol. Chem. , vol.277 , pp. 25096-25105
    • Obst, M.1    Oppermann-Sanio, F.B.2    Luftmann, H.3    Steinbuchel, A.4
  • 20
    • 44949198468 scopus 로고    scopus 로고
    • Anaerobic and aerobic degradation of cyanophycin by the denitrifying bacterium Pseudomonas alcaligenes strain DIP1 and role of three other coisolates in a mixed bacterial consortium
    • Sallam A., and Steinbuchel A. Anaerobic and aerobic degradation of cyanophycin by the denitrifying bacterium Pseudomonas alcaligenes strain DIP1 and role of three other coisolates in a mixed bacterial consortium. Appl. Environ. Microbiol. 74 (2008) 3434-3443
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 3434-3443
    • Sallam, A.1    Steinbuchel, A.2
  • 21
    • 58149359424 scopus 로고    scopus 로고
    • Biotechnological process for production of beta-dipeptides from cyanophycin on a technical scale and its optimization
    • Sallam A., Kast A., Przybilla S., Meiswinkel T., and Steinbuchel A. Biotechnological process for production of beta-dipeptides from cyanophycin on a technical scale and its optimization. Appl. Environ. Microbiol. 75 (2009) 29-38
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 29-38
    • Sallam, A.1    Kast, A.2    Przybilla, S.3    Meiswinkel, T.4    Steinbuchel, A.5
  • 22
    • 0033559558 scopus 로고    scopus 로고
    • Structural and energetic determinants of the S1-site specificity in serine proteases
    • Czapinska H., and Otlewski J. Structural and energetic determinants of the S1-site specificity in serine proteases. Eur. J. Biochem. 260 (1999) 571-595
    • (1999) Eur. J. Biochem. , vol.260 , pp. 571-595
    • Czapinska, H.1    Otlewski, J.2
  • 23
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • Hedstrom L. Serine protease mechanism and specificity. Chem. Rev. 102 (2002) 4501-4524
    • (2002) Chem. Rev. , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 26
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., and Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372 (2007) 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 28
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L., and Sander C. Mapping the protein universe. Science 273 (1996) 595-603
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 29
    • 0032523821 scopus 로고    scopus 로고
    • Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-l-arginyl-poly-l-aspartate (cyanophycin)
    • Ziegler K., Diener A., Herpin C., Richter R., Deutzmann R., and Lockau W. Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-l-arginyl-poly-l-aspartate (cyanophycin). Eur. J. Biochem. 254 (1998) 154-159
    • (1998) Eur. J. Biochem. , vol.254 , pp. 154-159
    • Ziegler, K.1    Diener, A.2    Herpin, C.3    Richter, R.4    Deutzmann, R.5    Lockau, W.6
  • 30
    • 0036803980 scopus 로고    scopus 로고
    • The strand-helix motif is a recurring theme in biological hydrolysis. Does the conformation of the Ramachandran outlier enhance its electrophilicity?
    • Hakansson K. The strand-helix motif is a recurring theme in biological hydrolysis. Does the conformation of the Ramachandran outlier enhance its electrophilicity?. Int. J. Biol. Macromol. 30 (2002) 273-277
    • (2002) Int. J. Biol. Macromol. , vol.30 , pp. 273-277
    • Hakansson, K.1
  • 31
    • 0032578355 scopus 로고    scopus 로고
    • The 0.78 Å structure of a serine protease: Bacillus lentus subtilisin
    • Kuhn P., Knapp M., Soltis S.M., Ganshaw G., Thoene M., and Bott R. The 0.78 Å structure of a serine protease: Bacillus lentus subtilisin. Biochemistry 37 (1998) 13446-13452
    • (1998) Biochemistry , vol.37 , pp. 13446-13452
    • Kuhn, P.1    Knapp, M.2    Soltis, S.M.3    Ganshaw, G.4    Thoene, M.5    Bott, R.6
  • 32
    • 0041620372 scopus 로고    scopus 로고
    • Annotation in three dimensions. PINTS: patterns in non-homologous tertiary structures
    • Stark A., and Russell R.B. Annotation in three dimensions. PINTS: patterns in non-homologous tertiary structures. Nucleic Acids Res. 31 (2003) 3341-3344
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3341-3344
    • Stark, A.1    Russell, R.B.2
  • 33
    • 33749247217 scopus 로고    scopus 로고
    • Crystal structure at 1.9 Å of E. coli ClpP with a peptide covalently bound at the active site
    • Szyk A., and Maurizi M.R. Crystal structure at 1.9 Å of E. coli ClpP with a peptide covalently bound at the active site. J. Struct. Biol. 156 (2006) 165-174
    • (2006) J. Struct. Biol. , vol.156 , pp. 165-174
    • Szyk, A.1    Maurizi, M.R.2
  • 34
    • 44149116183 scopus 로고    scopus 로고
    • The structural basis for the activation and peptide recognition of bacterial ClpP
    • Kim D.Y., and Kim K.K. The structural basis for the activation and peptide recognition of bacterial ClpP. J. Mol. Biol. 379 (2008) 760-771
    • (2008) J. Mol. Biol. , vol.379 , pp. 760-771
    • Kim, D.Y.1    Kim, K.K.2
  • 35
    • 0028168468 scopus 로고
    • (His)C epsilon-H...O = C < hydrogen bond in the active sites of serine hydrolases
    • Derewenda Z.S., Derewenda U., and Kobos P.M. (His)C epsilon-H...O = C < hydrogen bond in the active sites of serine hydrolases. J. Mol. Biol. 241 (1994) 83-93
    • (1994) J. Mol. Biol. , vol.241 , pp. 83-93
    • Derewenda, Z.S.1    Derewenda, U.2    Kobos, P.M.3
  • 36
    • 0034641613 scopus 로고    scopus 로고
    • 1H NMR chemical shifts support (His) C(epsilon) 1...O {double bond, long} C H-bond: proposal for reaction-driven ring flip mechanism in serine protease catalysis
    • 1H NMR chemical shifts support (His) C(epsilon) 1...O {double bond, long} C H-bond: proposal for reaction-driven ring flip mechanism in serine protease catalysis. Proc. Natl Acad. Sci. USA 97 (2000) 10371-10376
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10371-10376
    • Ash, E.L.1    Sudmeier, J.L.2    Day, R.M.3    Vincent, M.4    Torchilin, E.V.5    Haddad, K.C.6
  • 37
    • 0032574704 scopus 로고    scopus 로고
    • Site-directed mutagenesis probing the catalytic role of arginines 165 and 166 of human cytomegalovirus protease
    • Liang P.H., Brun K.A., Feild J.A., O'Donnell K., Doyle M.L., Green S.M., et al. Site-directed mutagenesis probing the catalytic role of arginines 165 and 166 of human cytomegalovirus protease. Biochemistry 37 (1998) 5923-5929
    • (1998) Biochemistry , vol.37 , pp. 5923-5929
    • Liang, P.H.1    Brun, K.A.2    Feild, J.A.3    O'Donnell, K.4    Doyle, M.L.5    Green, S.M.6
  • 39
    • 27144523783 scopus 로고    scopus 로고
    • The catalytic triad of serine peptidases
    • Polgar L. The catalytic triad of serine peptidases. Cell. Mol. Life Sci. 62 (2005) 2161-2172
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2161-2172
    • Polgar, L.1
  • 40
    • 17244364283 scopus 로고    scopus 로고
    • Proteases universally recognize beta strands in their active sites
    • Tyndall J.D., Nall T., and Fairlie D.P. Proteases universally recognize beta strands in their active sites. Chem. Rev. 105 (2005) 973-999
    • (2005) Chem. Rev. , vol.105 , pp. 973-999
    • Tyndall, J.D.1    Nall, T.2    Fairlie, D.P.3
  • 42
    • 0035339420 scopus 로고    scopus 로고
    • A ninhydrin-based assay to quantitate the total protein content of tissue samples
    • Starcher B. A ninhydrin-based assay to quantitate the total protein content of tissue samples. Anal. Biochem. 292 (2001) 125-129
    • (2001) Anal. Biochem. , vol.292 , pp. 125-129
    • Starcher, B.1
  • 43
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes
    • Minor W., Cymborowski M., Otwinowski Z., and Chruszcz M. HKL-3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes. Acta Crystallogr., Sect. D: Biol. Crystallogr. 62 (2006) 859-866
    • (2006) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 45
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris R.J., Perrakis A., and Lamzin V.S. ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol. 374 (2003) 229-244
    • (2003) Methods Enzymol. , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 46
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 47
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.