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Volumn 77, Issue 6, 2011, Pages 2019-2025

Poly-α-glutamic acid synthesis using a novel catalytic activity of Rimk from Escherichia coli K-12

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE LINKAGES; C TERMINUS; CATALYTIC ACTIVITY; CYANOPHYCIN; GLUTAMIC ACID; L-AMINO ACIDS; L-GLUTAMIC ACIDS; MATRIX-ASSISTED LASER DESORPTION IONIZATION; PEPTIDE ELONGATION; RIBOSOMAL PROTEINS; SUBSTRATE SPECIFICITY; THERMAL STABILITY; TIME OF FLIGHT;

EID: 79953185761     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02043-10     Document Type: Article
Times cited : (33)

References (33)
  • 1
    • 84985059113 scopus 로고
    • Papain-induced oligomerization of α-amino acid esters
    • Anderson, G., and P. L. Luisi. 1979. Papain-induced oligomerization of α-amino acid esters. Helv. Chim. Acta. 62:488-494.
    • (1979) Helv. Chim. Acta. , vol.62 , pp. 488-494
    • Anderson, G.1    Luisi, P.L.2
  • 2
    • 56749183302 scopus 로고    scopus 로고
    • A novel L-amino acid ligase is encoded by a gene in the phaseolotoxin biosynthetic gene cluster from Pseudomonas syringae pv. phaseolicola 1448A
    • Arai, T., and K. Kino. 2008. A novel L-amino acid ligase is encoded by a gene in the phaseolotoxin biosynthetic gene cluster from Pseudomonas syringae pv. phaseolicola 1448A. Biosci. Biotechnol. Biochem. 72:3048-3050.
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 3048-3050
    • Arai, T.1    Kino, K.2
  • 3
    • 54349098431 scopus 로고    scopus 로고
    • A cyanophycin synthetase from Thermosynechococcus elongatus BP-1 catalyzes primer-independent cyanophycin synthesis
    • Arai, T., and K. Kino. 2008. A cyanophycin synthetase from Thermosynechococcus elongatus BP-1 catalyzes primer-independent cyanophycin synthesis. Appl. Microbiol. Biotechnol. 81:69-78.
    • (2008) Appl. Microbiol. Biotechnol. , vol.81 , pp. 69-78
    • Arai, T.1    Kino, K.2
  • 4
    • 77956029899 scopus 로고    scopus 로고
    • New L-amino acid ligases catalyzing oligopeptide synthesis from various microorganisms
    • Arai, T., and K. Kino. 2010. New L-amino acid ligases catalyzing oligopeptide synthesis from various microorganisms. Biosci. Biotechnol. Biochem. 74: 1572-1577.
    • (2010) Biosci. Biotechnol. Biochem. , vol.74 , pp. 1572-1577
    • Arai, T.1    Kino, K.2
  • 5
    • 0036323007 scopus 로고    scopus 로고
    • Biochemistry and molecular genetics of poly-gamma-glutamate synthesis
    • Ashiuchi, M., and H. Misono. 2002. Biochemistry and molecular genetics of poly-gamma-glutamate synthesis. Appl. Microbiol. Biotechnol. 59:9-14.
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 9-14
    • Ashiuchi, M.1    Misono, H.2
  • 6
    • 33745289074 scopus 로고    scopus 로고
    • Poly-gamma-glutamate in bacteria
    • Candela, T., and A. Fouet. 2006. Poly-gamma-glutamate in bacteria. Mol. Microbiol. 60:1091-1098.
    • (2006) Mol. Microbiol. , vol.60 , pp. 1091-1098
    • Candela, T.1    Fouet, A.2
  • 7
    • 0141942114 scopus 로고    scopus 로고
    • Membrane permeability commonly shared among arginine-rich peptides
    • Futaki, S., S. Goto, and Y. Sugiura. 2003. Membrane permeability commonly shared among arginine-rich peptides. J. Mol. Recognit. 16:260-264.
    • (2003) J. Mol. Recognit. , vol.16 , pp. 260-264
    • Futaki, S.1    Goto, S.2    Sugiura, Y.3
  • 8
    • 0031467818 scopus 로고    scopus 로고
    • A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity
    • Galperin, M. Y., and E. V. Koonin. 1997. A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Protein Sci. 6:2639-2643.
    • (1997) Protein Sci , vol.6 , pp. 2639-2643
    • Galperin, M.Y.1    Koonin, E.V.2
  • 9
    • 69249152207 scopus 로고    scopus 로고
    • Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus
    • Horie, A., et al. 2009. Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus. Nat. Chem. Biol. 5:673-679.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 673-679
    • Horie, A.1
  • 10
    • 48449090786 scopus 로고    scopus 로고
    • NCBI BLAST: a better web interface
    • Johnson, M., et al. 2008. NCBI BLAST: a better web interface. Nucleic Acids Res. 36:W5-W9.
    • (2008) Nucleic Acids Res , vol.36
    • Johnson, M.1
  • 11
    • 84985108854 scopus 로고
    • Papain catalyzed oligomerization of α-amino acid. Synthesis and characterization of water-insoluble oligomers of L-methionine
    • Jost, R., E. Brambilla, and J. C. Monti. 1980. Papain catalyzed oligomerization of (-amino acid. Synthesis and characterization of water-insoluble oligomers of L-methionine. Helv. Chim. Acta 63:375-384.
    • (1980) Helv. Chim. Acta , vol.63 , pp. 375-384
    • Jost, R.1    Brambilla, E.2    Monti, J.C.3
  • 12
    • 34548728025 scopus 로고    scopus 로고
    • Ribosome biogenesis and the translation process in Escherichia coli
    • Kaczanowska, M., and M. Rydén-Aulin. 2007. Ribosome biogenesis and the translation process in Escherichia coli. Microbiol. Mol. Biol. Rev. 71:477- 494.
    • (2007) Microbiol. Mol. Biol. Rev. , vol.71 , pp. 477-494
    • Kaczanowska, M.1    Rydén-Aulin, M.2
  • 13
    • 0024674214 scopus 로고
    • Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12
    • Kang, W. K., T. Icho, S. Isono, M. Kitakawa, and K. Isono. 1989. Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12. Mol. Gen. Genet. 217:281-288.
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 281-288
    • Kang, W.K.1    Icho, T.2    Isono, S.3    Kitakawa, M.4    Isono, K.5
  • 14
    • 33751538620 scopus 로고    scopus 로고
    • Novel substrate specificity of glutathione synthesis enzymes from Streptococcus agalactiae and Clostridium acetobutylicum
    • Kino, K., et al. 2007. Novel substrate specificity of glutathione synthesis enzymes from Streptococcus agalactiae and Clostridium acetobutylicum. Biochem. Biophys. Res. Commun. 352:351-359.
    • (2007) Biochem. Biophys. Res. Commun. , vol.352 , pp. 351-359
    • Kino, K.1
  • 15
    • 75649144445 scopus 로고    scopus 로고
    • A novel L-amino acid ligase from Bacillus subtilis NBRC3134 catalyzed oligopeptide synthesis
    • Kino, K., T. Arai, and D. Tateiwa. 2010. A novel L-amino acid ligase from Bacillus subtilis NBRC3134 catalyzed oligopeptide synthesis. Biosci. Biotechnol. Biochem. 74:129-134.
    • (2010) Biosci. Biotechnol. Biochem. , vol.74 , pp. 129-134
    • Kino, K.1    Arai, T.2    Tateiwa, D.3
  • 16
    • 67149125327 scopus 로고    scopus 로고
    • A novel L-amino acid ligase from Bacillus subtilis NBRC3134, a microorganism producing peptideantibiotic rhizocticin
    • Kino, K., Y. Kotanaka, T. Arai, and M. Yagasaki. 2009. A novel L-amino acid ligase from Bacillus subtilis NBRC3134, a microorganism producing peptideantibiotic rhizocticin. Biosci. Biotechnol. Biochem. 73:901-907.
    • (2009) Biosci. Biotechnol. Biochem. , vol.73 , pp. 901-907
    • Kino, K.1    Kotanaka, Y.2    Arai, T.3    Yagasaki, M.4
  • 17
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 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
  • 19
    • 0042191785 scopus 로고    scopus 로고
    • Glutathione synthetase homologs encode α-L-glutamate ligases for methanogenic coenzyme F420 and tetrahydrosarcinapterin biosyntheses
    • Li, H., H. Xu, D. E. Graham, and R. H. White. 2003. Glutathione synthetase homologs encode (-L-glutamate ligases for methanogenic coenzyme F420 and tetrahydrosarcinapterin biosyntheses. Proc. Natl. Acad. Sci. U. S. A. 100:9785-9790.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 9785-9790
    • Li, H.1    Xu, H.2    Graham, D.E.3    White, R.H.4
  • 20
    • 77953487990 scopus 로고    scopus 로고
    • A novel method for the selective recovery and purification of gamma-polyglutamic acid from Bacillus licheniformis fermentation broth
    • Manocha, B., and A. Margaritis. 2010. A novel method for the selective recovery and purification of gamma-polyglutamic acid from Bacillus licheniformis fermentation broth. Biotechnol. Prog. 26:734-742.
    • (2010) Biotechnol. Prog. , vol.26 , pp. 734-742
    • Manocha, B.1    Margaritis, A.2
  • 21
    • 35649003888 scopus 로고    scopus 로고
    • Assessment of technological options and economical feasibility for cyanophycin biopolymer and high-value amino acid production
    • Mooibroek, H., et al. 2007. Assessment of technological options and economical feasibility for cyanophycin biopolymer and high-value amino acid production. Appl. Microbiol. Biotechnol. 77:257-267.
    • (2007) Appl. Microbiol. Biotechnol. , vol.77 , pp. 257-267
    • Mooibroek, H.1
  • 22
    • 0042736814 scopus 로고    scopus 로고
    • Crystal structure of a lysine biosynthesis enzyme, LysX, from Thermus thermophilus HB8
    • Sakai, H., et al. 2003. Crystal structure of a lysine biosynthesis enzyme, LysX, from Thermus thermophilus HB8. J. Mol. Biol. 332:729-740.
    • (2003) J. Mol. Biol. , vol.332 , pp. 729-740
    • Sakai, H.1
  • 24
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schägger, H. 2006. Tricine-SDS-PAGE. Nat. Protoc. 1:16-22.
    • (2006) Nat. Protoc. , vol.1 , pp. 16-22
    • Schägger, H.1
  • 25
    • 0031599328 scopus 로고    scopus 로고
    • Chemical synthesis of polyaspartates: a biodegradable alternative to currently used polycarboxylate homo- and copolymers
    • Schwamborn, M. 1998. Chemical synthesis of polyaspartates: a biodegradable alternative to currently used polycarboxylate homo- and copolymers. Polym. Degrad. Stab. 59:39-45.
    • (1998) Polym. Degrad. Stab. , vol.59 , pp. 39-45
    • Schwamborn, M.1
  • 26
    • 33645039015 scopus 로고    scopus 로고
    • Microbial synthesis of poly(epsilon-lysine) and its various applications
    • Shih, I. L., M. H. Shen, and Y. T. Van. 2006. Microbial synthesis of poly(epsilon-lysine) and its various applications. Bioresour. Technol. 97:1148- 1159.
    • (2006) Bioresour. Technol. , vol.97 , pp. 1148-1159
    • Shih, I.L.1    Shen, M.H.2    Van, Y.T.3
  • 27
    • 3042723162 scopus 로고    scopus 로고
    • Biomedical applications of chemically and microbiologically synthesized poly(glutamic acid) and poly(lysine)
    • Shih, I. L., Y. T. Van, and M. H. Shen. 2004. Biomedical applications of chemically and microbiologically synthesized poly(glutamic acid) and poly(lysine). Mini Rev. Med. Chem. 4:179-188.
    • (2004) Mini Rev. Med. Chem. , vol.4 , pp. 179-188
    • Shih, I.L.1    Van, Y.T.2    Shen, M.H.3
  • 28
    • 0015501897 scopus 로고
    • Sigmoidal progress curves in the polymerization of leucine methyl ester catalyzed by papain
    • Sluyterman, L. A., and J. Wijdenes. 1972. Sigmoidal progress curves in the polymerization of leucine methyl ester catalyzed by papain. Biochim. Biophys. Acta. 289:194-202.
    • (1972) Biochim. Biophys. Acta. , vol.289 , pp. 194-202
    • Sluyterman, L.A.1    Wijdenes, J.2
  • 29
    • 0343286276 scopus 로고
    • Amino acid-activating enzymes: methods of assay
    • Stulberg, P. M., and G. D. Novelli. 1962. Amino acid-activating enzymes: methods of assay. Methods Enzymol. 5:703-726.
    • (1962) Methods Enzymol , vol.5 , pp. 703-726
    • Stulberg, P.M.1    Novelli, G.D.2
  • 30
    • 22544447354 scopus 로고    scopus 로고
    • ywfE in Bacillus subtilis codes for a novel enzyme, L-amino acid ligase
    • Tabata, K., H. Ikeda, and S. Hashimoto. 2005. ywfE in Bacillus subtilis codes for a novel enzyme, L-amino acid ligase. J. Bacteriol. 187:5195-5202.
    • (2005) J. Bacteriol. , vol.187 , pp. 5195-5202
    • Tabata, K.1    Ikeda, H.2    Hashimoto, S.3
  • 31
    • 35448968675 scopus 로고    scopus 로고
    • Fermentative production of L-alanyl-L-glutamine by a metabolically engineered Escherichia coli strain expressing L-amino acid α-ligase
    • Tabata, K., and S. Hashimoto. 2007. Fermentative production of L-alanyl-L-glutamine by a metabolically engineered Escherichia coli strain expressing L-amino acid (-ligase. Appl. Environ. Microbiol. 73:6378-6385.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 6378-6385
    • Tabata, K.1    Hashimoto, S.2
  • 32
    • 0036198293 scopus 로고    scopus 로고
    • Protease-catalyzed regioselective polymerization and copolymerization of glutamic acid diethyl ester
    • Uyama, H., T. Fukuoka, I. Komatsu, T. Watanabe, and S. Kobayashi. 2002. Protease-catalyzed regioselective polymerization and copolymerization of glutamic acid diethyl ester. Biomacromolecules 3:318-323.
    • (2002) Biomacromolecules , vol.3 , pp. 318-323
    • Uyama, H.1    Fukuoka, T.2    Komatsu, I.3    Watanabe, T.4    Kobayashi, S.5
  • 33
    • 56249145109 scopus 로고    scopus 로고
    • Epsilonpoly-L-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase
    • Yamanaka, K., C. Maruyama, H. Takagi, and Y. Hamano. 2008. Epsilonpoly-L-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase. Nat. Chem. Biol. 4:766-772.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 766-772
    • Yamanaka, K.1    Maruyama, C.2    Takagi, H.3    Hamano, Y.4


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