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Volumn 29, Issue 9, 2015, Pages 4071-4079

New aminopeptidase from "microbial dark matter" archaeon

Author keywords

Carbon cycle; Detrital proteins; Marine sediments; Single cell genomics

Indexed keywords

ALANINE; AMINOPEPTIDASE; ARGININE; CYSTEINE; GLYCINE; ISOLEUCINE; LEUCINE; PHENYLALANINE; PYRIDINE; TRYPTOPHAN; TYROSINE; ARCHAEAL PROTEIN;

EID: 84965084826     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.15-272906     Document Type: Article
Times cited : (17)

References (41)
  • 3
    • 34547492897 scopus 로고    scopus 로고
    • Matching phylogeny and metabolism in the uncultured marine bacteria, one cell ata time
    • Stepanauskas, R., and Sieracki, M. E. (2007) Matching phylogeny and metabolism in the uncultured marine bacteria, one cell ata time. Proc. Natl. Acad. Sci. USA 104,9052-9057
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 9052-9057
    • Stepanauskas, R.1    Sieracki, M.E.2
  • 6
    • 84894363922 scopus 로고    scopus 로고
    • Genetic and functional properties of uncultivated MCG archaea assessed by metagenome and gene expression analyses
    • Meng, J., Xu, J., Qin, D., He, Y., Xiao, X., and Wang, F. (2014) Genetic and functional properties of uncultivated MCG archaea assessed by metagenome and gene expression analyses. ISME J. 8, 650-659
    • (2014) ISME J , vol.8 , pp. 650-659
    • Meng, J.1    Xu, J.2    Qin, D.3    He, Y.4    Xiao, X.5    Wang, F.6
  • 8
    • 0036772305 scopus 로고    scopus 로고
    • The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis
    • Rigolet, P., Mechin, I., Delage, M. M., and Chich, J. F. (2002) The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis. Structure 10, 1383-1394
    • (2002) Structure , vol.10 , pp. 1383-1394
    • Rigolet, P.1    Mechin, I.2    Delage, M.M.3    Chich, J.F.4
  • 9
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • Hedstrom, L. (2002) Serine protease mechanism and specificity. Chem. Rev. 102, 4501-4524
    • (2002) Chem. Rev , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 11
    • 0025560063 scopus 로고
    • Intracellular aminopeptidase from Xanthomonas rubrilineans, hydrolyzing alphaamino acid esters and cefalexin
    • Krest'ianova, I. N., Uvarov, N. N., Rudenskaia, G. N., Tsibanov, V. V., Vasil'eva, L. I., and Stepanov, V. M. (1990) [Intracellular aminopeptidase from Xanthomonas rubrilineans, hydrolyzing alphaamino acid esters and cefalexin]. Biokhimiia 55,2226-2238
    • (1990) Biokhimiia , vol.55 , pp. 2226-2238
    • Krest'Ianova, I.N.1    Uvarov, N.N.2    Rudenskaia, G.N.3    Tsibanov, V.V.4    Vasil'Eva, L.I.5    Stepanov, V.M.6
  • 12
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • Aslanidis, C., and de Jong, P. J. (1990) Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res. 18, 6069-6074
    • (1990) Nucleic Acids Res , vol.18 , pp. 6069-6074
    • Aslanidis, C.1    De Jong, P.J.2
  • 13
    • 84934441968 scopus 로고    scopus 로고
    • A family of LIC vectors for high-throughput cloning and purification of proteins
    • Eschenfeldt, W. H., Lucy, S., Millard, C. S., Joachimiak, A., and Mark, I. D. (2009) A family of LIC vectors for high-throughput cloning and purification of proteins. Methods Mol. Biol. 498, 105-115
    • (2009) Methods Mol. Biol , vol.498 , pp. 105-115
    • Eschenfeldt, W.H.1    Lucy, S.2    Millard, C.S.3    Joachimiak, A.4    Mark, I.D.5
  • 15
    • 0036926615 scopus 로고    scopus 로고
    • A new vector for high-throughput, ligationindependent cloning encoding a tobacco etch virus protease cleavage site
    • Stols, L., Gu, M., Dieckman, L., Raffen, R., Collart, F. R., and Donnelly, M. I. (2002) A new vector for high-throughput, ligationindependent cloning encoding a tobacco etch virus protease cleavage site. Protein Expr. Purif. 25, 8-15
    • (2002) Protein Expr. Purif , vol.25 , pp. 8-15
    • Stols, L.1    Gu, M.2    Dieckman, L.3    Raffen, R.4    Collart, F.R.5    Donnelly, M.I.6
  • 16
    • 3543110895 scopus 로고    scopus 로고
    • Production of selenomethionine-labeled proteins in two-liter plastic bottles for structure determination
    • Stols, L., Millard, C. S., Dementieva, I., and Donnelly, M. I. (2004)Production of selenomethionine-labeled proteins in two-liter plastic bottles for structure determination. J. Struct. Funct. Genomics5,95-102
    • (2004) J. Struct. Funct. Genomics5 , pp. 95-102
    • Stols, L.1    Millard, C.S.2    Dementieva, I.3    Donnelly, M.I.4
  • 20
    • 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. (2006) HKL-3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes. Acta Crystallogr. D Biol. Crystallogr. 62,859-866
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 21
    • 0000952473 scopus 로고
    • Treatment of negative intensity observations
    • French, G. S., and Wilson, K. S. (1978) Treatment of negative intensity observations. Acta Crystallogr. A 34,517-525
    • (1978) Acta Crystallogr , vol.A34 , pp. 517-525
    • French, G.S.1    Wilson, K.S.2
  • 22
    • 0037779022 scopus 로고    scopus 로고
    • A statistic for local intensity differences: Robustness to anisotropy and pseudo-centering and utility for detecting twinning
    • Padilla, J. E., and Yeates, T. O. (2003) A statistic for local intensity differences: robustness to anisotropy and pseudo-centering and utility for detecting twinning. Acta Crystallogr. D Biol. Crystallogr. 59, 1124-1130
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 1124-1130
    • Padilla, J.E.1    Yeates, T.O.2
  • 24
    • 0038339247 scopus 로고    scopus 로고
    • The sequence and crystal structure of the alpha-amino acid ester hydrolase from Xanthomonas citri define a new family of beta-lactam antibiotic acylases
    • Barends, T. R., Polderman-Tijmes, J. J., Jekel, P. A., Hensgens, C. M., de Vries, E. J., Janssen, D. B., and Dijkstra, B. W. (2003) The sequence and crystal structure of the alpha-amino acid ester hydrolase from Xanthomonas citri define a new family of beta-lactam antibiotic acylases. J. Biol. Chem. 278, 23076-23084
    • (2003) J. Biol. Chem. , vol.278 , pp. 23076-23084
    • Barends, T.R.1    Polderman-Tijmes, J.J.2    Jekel, P.A.3    Hensgens, C.M.4    De Vries, E.J.5    Janssen, D.B.6    Dijkstra, B.W.7
  • 26
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer, G., Cohen, S. X., Lamzin, V. S., and Perrakis, A. (2008)Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc. 3, 1171-1179
    • (2008) Nat. Protoc , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 28
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn, M. D., Murshudov, G. N., and Papiz, M. Z. (2003) Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol. 374,300-321
    • (2003) Methods Enzymol , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 33
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: A multiple sequence alignment method with reduced time and space complexity
    • Edgar, R. C. (2004) MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 5,113
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1
  • 36
    • 0346432066 scopus 로고    scopus 로고
    • Acetobacter turbidans alpha-amino acid ester hydrolase: Merohedral twinning in P21 obscured by pseudo-translational NCS
    • Barends, T. R., and Dijkstra, B. W. (2003) Acetobacter turbidans alpha-amino acid ester hydrolase: merohedral twinning in P21 obscured by pseudo-translational NCS. Acta Crystallogr. D Biol. Crystallogr. 59, 2237-2241
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 2237-2241
    • Barends, T.R.1    Dijkstra, B.W.2
  • 38
    • 33646845162 scopus 로고    scopus 로고
    • Acetobacter turbidans alpha-amino acid ester hydrolase: How a single mutation improves an antibiotic-producing enzyme
    • Barends, T. R., Polderman-Tijmes, J. J., Jekel, P. A., Williams, C., Wybenga, G., Janssen, D. B., and Dijkstra, B. W. (2006) Acetobacter turbidans alpha-amino acid ester hydrolase: how a single mutation improves an antibiotic-producing enzyme. J. Biol. Chem. 281, 5804-5810
    • (2006) J. Biol. Chem. , vol.281 , pp. 5804-5810
    • Barends, T.R.1    Polderman-Tijmes, J.J.2    Jekel, P.A.3    Williams, C.4    Wybenga, G.5    Janssen, D.B.6    Dijkstra, B.W.7
  • 39
    • 0015693624 scopus 로고
    • The pKa values of the a-amino groups of peptides derived from the N-terminus of bovine growth hormone
    • Wallis, M. (1973) The pKa values of the a-amino groups of peptides derived from the N-terminus of bovine growth hormone. Biochim. Biophys. Acta 310,388-397
    • (1973) Biochim. Biophys. Acta , vol.310 , pp. 388-397
    • Wallis, M.1
  • 41
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Hot topics in cold adaptation
    • Feller, G., and Gerday, C. (2003) Psychrophilic enzymes: hot topics in cold adaptation. Nat. Rev. Microbiol. 1, 200-208
    • (2003) Nat. Rev. Microbiol , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.