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Volumn 72, Issue 6, 2006, Pages 4225-4231

Dipeptide synthesis by an aminopeptidase from Streptomyces septatus TH-2 and its application to synthesis of biologically active peptides

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ESTERS; METHANOL; MICROORGANISMS; REACTION KINETICS; SYNTHESIS (CHEMICAL);

EID: 33745163242     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.00150-06     Document Type: Article
Times cited : (29)

References (38)
  • 1
    • 1842531108 scopus 로고    scopus 로고
    • Gene cloning and overproduction of an aminopeptidase from Streptomyces septatus TH-2, and comparison with a calcium-activated enzyme from Streptomyces griseus
    • Arima, J., M. Iwabuchi, and T. Hatanaka. 2004. Gene cloning and overproduction of an aminopeptidase from Streptomyces septatus TH-2, and comparison with a calcium-activated enzyme from Streptomyces griseus. Biochem. Biophys. Res. Commun. 317:531-538.
    • (2004) Biochem. Biophys. Res. Commun. , vol.317 , pp. 531-538
    • Arima, J.1    Iwabuchi, M.2    Hatanaka, T.3
  • 2
    • 33645700889 scopus 로고    scopus 로고
    • Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica
    • Arima, J., Y. Uesugi, M. Iwabuchi, and T. Hatanaka. 2006. Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica. Appl. Microb. Biotechnol. 70:541-547.
    • (2006) Appl. Microb. Biotechnol. , vol.70 , pp. 541-547
    • Arima, J.1    Uesugi, Y.2    Iwabuchi, M.3    Hatanaka, T.4
  • 3
    • 31444450427 scopus 로고    scopus 로고
    • Alteration of leucine aminopeptidase from Streptomyces septatus TH-2 to phenylalanine aminopeptidase by site-directed mutagenesis
    • Arima, J., Y. Uesugi, M. Iwabuchi, and T. Hatanaka. 2005. Alteration of leucine aminopeptidase from Streptomyces septatus TH-2 to phenylalanine aminopeptidase by site-directed mutagenesis. Appl. Environ. Microbiol. 71: 7229-7235.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 7229-7235
    • Arima, J.1    Uesugi, Y.2    Iwabuchi, M.3    Hatanaka, T.4
  • 4
    • 33646851100 scopus 로고    scopus 로고
    • Modulation of Streptomyces leucine aminopeptidase by calcium: Identification and functional analysis of key residues in activation and stabilization by calcium
    • Arima, J., Y. Uesugi, M. Uraji, S. Yatsushiro, S. Tsuboi, M. Iwabuchi, and T. Hatanaka. 2006. Modulation of Streptomyces leucine aminopeptidase by calcium: identification and functional analysis of key residues in activation and stabilization by calcium. J. Biol. Chem. 281:5885-5894.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5885-5894
    • Arima, J.1    Uesugi, Y.2    Uraji, M.3    Yatsushiro, S.4    Tsuboi, S.5    Iwabuchi, M.6    Hatanaka, T.7
  • 5
    • 31444437640 scopus 로고    scopus 로고
    • The role of Glu196 in environment around substrate binding site of leucine aminopeptidase from Streptomyces griseus
    • Arima, J., Y. Uesugi, M. Uraji, M. Iwabuchi, and T. Hatanaka. 2006. The role of Glu196 in environment around substrate binding site of leucine aminopeptidase from Streptomyces griseus. FEBS Lett. 580:912-917.
    • (2006) FEBS Lett. , vol.580 , pp. 912-917
    • Arima, J.1    Uesugi, Y.2    Uraji, M.3    Iwabuchi, M.4    Hatanaka, T.5
  • 6
    • 1642332337 scopus 로고    scopus 로고
    • Characteristics of a new enantioselective thermostable dipeptidase from Brevibacillus borstelensis BCS-1 and its application to synthesis of a D-amino-acid-containing dipeptide
    • Baek, D. H., J. J. Song, S. J. Kwon, C. Park, C. M. Jung, and M. H. Sung. 2004. Characteristics of a new enantioselective thermostable dipeptidase from Brevibacillus borstelensis BCS-1 and its application to synthesis of a D-amino-acid-containing dipeptide. Appl. Environ. Microbiol. 70:1570-1575.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 1570-1575
    • Baek, D.H.1    Song, J.J.2    Kwon, S.J.3    Park, C.4    Jung, C.M.5    Sung, M.H.6
  • 7
    • 0036370771 scopus 로고    scopus 로고
    • The aminopeptidase from Aeromonas proteolytica can function as an esterase
    • Bienvenue, D. L., R. S. Mathew, D. Ringe, and R. C. Holz. 2002. The aminopeptidase from Aeromonas proteolytica can function as an esterase. J. Biol. Inorg. Chem. 7:129-135.
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 129-135
    • Bienvenue, D.L.1    Mathew, R.S.2    Ringe, D.3    Holz, R.C.4
  • 8
    • 3843081911 scopus 로고    scopus 로고
    • The catalytic role of glutamate 151 in the leucine aminopeptidase from Aeromonas proteolytica
    • Bzymek, K. P., and R. C. Holz. 2004. The catalytic role of glutamate 151 in the leucine aminopeptidase from Aeromonas proteolytica. J. Biol. Chem. 279:31018-31025.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31018-31025
    • Bzymek, K.P.1    Holz, R.C.2
  • 9
    • 0028773280 scopus 로고
    • Crystal structure of Aeromonas proteolytica aminopeptidase: A prototypical member of the co-catalytic zinc enzyme family
    • Chevrier, B., C. Schalk, H. D'Orchymont, J. M. Rondeau, D. Moras, and C. Tarnus. 1994. Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family. Structure 2:283-291.
    • (1994) Structure , vol.2 , pp. 283-291
    • Chevrier, B.1    Schalk, C.2    D'Orchymont, H.3    Rondeau, J.M.4    Moras, D.5    Tarnus, C.6
  • 10
    • 0018255396 scopus 로고
    • L-Alanyl-L-tyrosine as a tyrosine source during intravenous nutrition of the rat
    • Daabees, T. T., and L. D. Stegink. 1978. L-Alanyl-L-tyrosine as a tyrosine source during intravenous nutrition of the rat. J. Nutr. 108:1104-1113.
    • (1978) J. Nutr. , vol.108 , pp. 1104-1113
    • Daabees, T.T.1    Stegink, L.D.2
  • 11
    • 0018386172 scopus 로고
    • L-Alanyl-L-tyrosine as a tyrosine source during total parenteral nutrition. Infusion at 0.5 and 2 mmoles/kg/day in adult rats
    • Daabees, T. T., and L. D. Stegink. 1979. L-Alanyl-L-tyrosine as a tyrosine source during total parenteral nutrition. Infusion at 0.5 and 2 mmoles/kg/day in adult rats. Pediatr. Res. 13:894-899.
    • (1979) Pediatr. Res. , vol.13 , pp. 894-899
    • Daabees, T.T.1    Stegink, L.D.2
  • 12
    • 0033551445 scopus 로고    scopus 로고
    • 1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: A case of arrested development
    • De Paola, C. C., B. Bennett, R. C. Holz, D. Ringe, and G. A. Petsko. 1999. 1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development. Biochemistry 38:9048-9053.
    • (1999) Biochemistry , vol.38 , pp. 9048-9053
    • De Paola, C.C.1    Bennett, B.2    Holz, R.C.3    Ringe, D.4    Petsko, G.A.5
  • 13
    • 0036691521 scopus 로고    scopus 로고
    • The 1.20 À resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with tris: A tale of buffer inhibition
    • Desmarais, W. T., D. L. Bienvenue, K. P. Bzymek, R. C. Holz, G. A. Petsko, and D. Ringe. 2002. The 1.20 À resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with tris: a tale of buffer inhibition. Structure 10:1063-1072.
    • (2002) Structure , vol.10 , pp. 1063-1072
    • Desmarais, W.T.1    Bienvenue, D.L.2    Bzymek, K.P.3    Holz, R.C.4    Petsko, G.A.5    Ringe, D.6
  • 14
    • 0345305853 scopus 로고    scopus 로고
    • Construction of hybrid peptide synthetases for the production of alpha-L-aspartyl-L-phenylalanine, a precursor for the high-intensity sweetener aspartame
    • Duerfahrt, T., S. Doekel, T. Sonke, P. J. Quaedflieg, and M. A. Marahiel. 2003. Construction of hybrid peptide synthetases for the production of alpha-L-aspartyl-L-phenylalanine, a precursor for the high-intensity sweetener aspartame. Eur. J. Biochem. 270:4555-4563.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4555-4563
    • Duerfahrt, T.1    Doekel, S.2    Sonke, T.3    Quaedflieg, P.J.4    Marahiel, M.A.5
  • 15
    • 3342995026 scopus 로고    scopus 로고
    • Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus
    • Fundoiano-Hershcovitz, Y., L. Rabinovitch, Y. Langut, V. Reiland, G. Shoham, and Y. Shoham. 2004. Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus. FEBS Lett. 571:192-196.
    • (2004) FEBS Lett. , vol.571 , pp. 192-196
    • Fundoiano-Hershcovitz, Y.1    Rabinovitch, L.2    Langut, Y.3    Reiland, V.4    Shoham, G.5    Shoham, Y.6
  • 17
    • 0035451816 scopus 로고    scopus 로고
    • Interactions of Streptomyces griseus aminopeptidase with amino acid reaction products and their implications toward a catalytic mechanism
    • Gilboa, R., A. Spungin-Bialik, G. Wohlfahrt, D. Schomburg, S. Blumberg, and G. Shoham. 2001. Interactions of Streptomyces griseus aminopeptidase with amino acid reaction products and their implications toward a catalytic mechanism. Proteins 44:490-504.
    • (2001) Proteins , vol.44 , pp. 490-504
    • Gilboa, R.1    Spungin-Bialik, A.2    Wohlfahrt, G.3    Schomburg, D.4    Blumberg, S.5    Shoham, G.6
  • 19
    • 0028788066 scopus 로고
    • Synthesis of cysteine-containing dipeptides by amino-acyl-tRNA synthetases
    • Jakubowski, H. 1995. Synthesis of cysteine-containing dipeptides by amino-acyl-tRNA synthetases. Nucleic Acids Res. 23:4608-4615.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4608-4615
    • Jakubowski, H.1
  • 21
    • 0036882401 scopus 로고    scopus 로고
    • Metalloaminopeptidases: Common functional themes in disparate structural surroundings
    • Lowther, W. T., and B. W. Matthews. 2002. Metalloaminopeptidases: common functional themes in disparate structural surroundings. Chem. Rev. 102:4581-4607.
    • (2002) Chem. Rev. , vol.102 , pp. 4581-4607
    • Lowther, W.T.1    Matthews, B.W.2
  • 22
    • 0031280027 scopus 로고    scopus 로고
    • Insertion of stabilizing loci in vectors of T7 RNA polymerase-mediated Escherichia coli expression systems: A case study on the plasmids involving foreign phospholipase D gene
    • Mishima, N., K. Mizumoto, Y. Iwasaki, H. Nakano, and T. Yamane. 1997. Insertion of stabilizing loci in vectors of T7 RNA polymerase-mediated Escherichia coli expression systems: a case study on the plasmids involving foreign phospholipase D gene. Biotechnol. Prog. 13:864-868.
    • (1997) Biotechnol. Prog. , vol.13 , pp. 864-868
    • Mishima, N.1    Mizumoto, K.2    Iwasaki, Y.3    Nakano, H.4    Yamane, T.5
  • 23
    • 0014828815 scopus 로고
    • Thermolysin: Kinetic study with oligopeptides
    • Morihara, K., and H. Tsuzuki. 1970. Thermolysin: kinetic study with oligopeptides. Eur. J. Biochem. 15:374-380.
    • (1970) Eur. J. Biochem. , vol.15 , pp. 374-380
    • Morihara, K.1    Tsuzuki, H.2
  • 24
    • 0025611814 scopus 로고
    • Continuous peptide synthesis in a water-immiscible organic solvent with an immobilized enzyme
    • Nakanishi, K., and R. Matsuno. 1990. Continuous peptide synthesis in a water-immiscible organic solvent with an immobilized enzyme. Ann. N. Y. Acad. Sci. 613:652-655.
    • (1990) Ann. N. Y. Acad. Sci. , vol.613 , pp. 652-655
    • Nakanishi, K.1    Matsuno, R.2
  • 25
    • 0019057814 scopus 로고
    • Peptide bond synthesis catalyzed by thermolysin
    • Oka, T., and K. Morihara. 1980. Peptide bond synthesis catalyzed by thermolysin. J. Biochem. 88:807-813.
    • (1980) J. Biochem. , vol.88 , pp. 807-813
    • Oka, T.1    Morihara, K.2
  • 26
    • 0030960777 scopus 로고    scopus 로고
    • D-Alanyl-D-lactate and D-alanyl-D-alanine synthesis by D-alanyl-D-alanine ligase from vancomycin-resistant Leuconostoc mesenteroides. Effects of a phenylalanine 261 to tyrosine mutation
    • Park, I. S., and C. T. Walsh. 1997. D-Alanyl-D-lactate and D-alanyl-D-alanine synthesis by D-alanyl-D-alanine ligase from vancomycin-resistant Leuconostoc mesenteroides. Effects of a phenylalanine 261 to tyrosine mutation. J. Biol. Chem. 272:9210-9214.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9210-9214
    • Park, I.S.1    Walsh, C.T.2
  • 29
    • 0022533191 scopus 로고
    • Reaction mechanism, specificity and pH-dependence of peptide synthesis catalyzed by the metalloproteinase thermolysin
    • Riechmann, L., and V. Kasche. 1986. Reaction mechanism, specificity and pH-dependence of peptide synthesis catalyzed by the metalloproteinase thermolysin. Biochim. Biophys. Acta 8723:269-276.
    • (1986) Biochim. Biophys. Acta , vol.8723 , pp. 269-276
    • Riechmann, L.1    Kasche, V.2
  • 31
    • 0019224215 scopus 로고
    • Effects of tyrosyl-arginine (kyotorphin), a new opioid dipeptide, on single neurons in the spinal dorsal horn of rabbits and the nucleus reticularis paragigantocellularis of rats
    • Satoh, M., S. Kawajiri, M. Yamamoto, A. Akaike, Y. Ukai, and H. Takagi. 1980. Effects of tyrosyl-arginine (kyotorphin), a new opioid dipeptide, on single neurons in the spinal dorsal horn of rabbits and the nucleus reticularis paragigantocellularis of rats. Neurosci. Lett. 16:319-322.
    • (1980) Neurosci. Lett. , vol.16 , pp. 319-322
    • Satoh, M.1    Kawajiri, S.2    Yamamoto, M.3    Akaike, A.4    Ukai, Y.5    Takagi, H.6
  • 32
    • 0027479013 scopus 로고
    • Aminopeptidases: Structure and function
    • Taylor, A. 1993. Aminopeptidases: structure and function. FASEB J. 7:290-298.
    • (1993) FASEB J. , vol.7 , pp. 290-298
    • Taylor, A.1
  • 33
    • 0027208935 scopus 로고
    • Aminopeptidase: Towards a mechanism of action
    • Taylor, A. 1993. Aminopeptidase: towards a mechanism of action. Trends Biochem. Sci. 18:167-172.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 167-172
    • Taylor, A.1
  • 34
    • 0003610748 scopus 로고    scopus 로고
    • Landes Bioscience Publishers, Austin, Tex.
    • Taylor, A. 1996. Aminopeptidases, p. 1-20. Landes Bioscience Publishers, Austin, Tex.
    • (1996) Aminopeptidases , pp. 1-20
    • Taylor, A.1
  • 36
    • 0015522498 scopus 로고
    • Specificity of Aeromonas aminopeptidase toward amino acid amides and dipeptides
    • Wagner, F. W., S. H. Wilkes, and J. M. Prescott. 1972. Specificity of Aeromonas aminopeptidase toward amino acid amides and dipeptides. J. Biol. Chem. 247:1208-1210.
    • (1972) J. Biol. Chem. , vol.247 , pp. 1208-1210
    • Wagner, F.W.1    Wilkes, S.H.2    Prescott, J.M.3
  • 37
    • 0342733342 scopus 로고
    • Thermolysin-catalyzed peptide bond synthesis
    • Wayne, S. I., and J. S. Fruton. 1983. Thermolysin-catalyzed peptide bond synthesis. Proc. Natl. Acad. Sci. USA 80:3241-3244.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 3241-3244
    • Wayne, S.I.1    Fruton, J.S.2
  • 38
    • 10644275942 scopus 로고    scopus 로고
    • A novel and efficient enzymatic method for the production of peptides from unprotected starting materials
    • Yokozeki, K., and S. Hara. 2005. A novel and efficient enzymatic method for the production of peptides from unprotected starting materials. J. Biotechnol. 115:211-220.
    • (2005) J. Biotechnol. , vol.115 , pp. 211-220
    • Yokozeki, K.1    Hara, S.2


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