메뉴 건너뛰기




Volumn 580, Issue 3, 2006, Pages 912-917

The role of Glu196 in the environment around the substrate binding site of leucine aminopeptidase from Streptomyces griseus

Author keywords

Activation by calcium; Glu196; Leucine aminopeptidase; Saturation mutagenesis; Streptomyces; Substrate specificity

Indexed keywords

CYTOSOL AMINOPEPTIDASE;

EID: 31444437640     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.01.014     Document Type: Article
Times cited : (7)

References (29)
  • 2
    • 0027208935 scopus 로고
    • Aminopeptidase: Towards a mechanism of action
    • A. Taylor Aminopeptidase: towards a mechanism of action Trends Biochem. Sci. 18 1993 167 172
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 167-172
    • Taylor, A.1
  • 3
    • 0027479013 scopus 로고
    • Aminopeptidases: Structure and function
    • A. Taylor Aminopeptidases: structure and function FASEB J. 7 1993 290 298
    • (1993) FASEB J. , vol.7 , pp. 290-298
    • Taylor, A.1
  • 4
    • 0003610748 scopus 로고    scopus 로고
    • Landes Bioscience Publishers Austin, TX
    • A. Taylor Aminopeptidases 1996 Landes Bioscience Publishers Austin, TX pp. 1-20
    • (1996) Aminopeptidases
    • Taylor, A.1
  • 5
    • 0036882401 scopus 로고    scopus 로고
    • Metalloaminopeptidases: Common functional themes in disparate structural surroundings
    • W.T. Lowther, and B.W. Matthews Metalloaminopeptidases: common functional themes in disparate structural surroundings Chem. Rev. 102 2002 4581 4607
    • (2002) Chem. Rev. , vol.102 , pp. 4581-4607
    • Lowther, W.T.1    Matthews, B.W.2
  • 6
    • 31444452433 scopus 로고    scopus 로고
    • Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica
    • (in press).
    • Arima, J., Uesugi, Y., Iwabuchi, M., and Hatanaka, T. (2005) Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica. Appl. Microb. Biotechnol. (in press).
    • (2005) Appl. Microb. Biotechnol.
    • Arima, J.1    Uesugi, Y.2    Iwabuchi, M.3    Hatanaka, T.4
  • 7
    • 0028773280 scopus 로고
    • Crystal structure of Aeromonas proteolytica aminopeptidase: A prototypical member of the co-catalytic zinc enzyme family
    • B. Chevrier, C. Schalk, H. D'Orchymont, J.M. Rondeau, D. Moras, and C. Tarnus Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family Structure 2 1994 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
  • 8
    • 0029989520 scopus 로고    scopus 로고
    • Aminopeptidase from Streptomyces griseus: Primary structure and comparison with other zinc-containing aminopeptidases
    • B. Maras, H.M. Greenblatt, G. Shoham, A. Spungin-Bialik, S. Blumberg, and D. Barra Aminopeptidase from Streptomyces griseus: primary structure and comparison with other zinc-containing aminopeptidases Eur. J. Biochem. 236 1996 843 846
    • (1996) Eur. J. Biochem. , vol.236 , pp. 843-846
    • Maras, B.1    Greenblatt, H.M.2    Shoham, G.3    Spungin-Bialik, A.4    Blumberg, S.5    Barra, D.6
  • 11
  • 12
    • 0033551445 scopus 로고    scopus 로고
    • 1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: A case of arrested development
    • C.C. De Paola, B. Bennett, R.C. Holz, D. Ringe, and G.A. Petsko 1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development Biochemistry 38 1999 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
    • 0035912827 scopus 로고    scopus 로고
    • Inhibition of the aminopeptidase from Aeromonas proteolytica by l-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis
    • C.C. Stamper, B. Bennett, T. Edwards, R.C. Holz, D. Ringe, and G. Petsko Inhibition of the aminopeptidase from Aeromonas proteolytica by l-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis Biochemistry 40 2001 7035 7046
    • (2001) Biochemistry , vol.40 , pp. 7035-7046
    • Stamper, C.C.1    Bennett, B.2    Edwards, T.3    Holz, R.C.4    Ringe, D.5    Petsko, G.6
  • 14
    • 3342926039 scopus 로고    scopus 로고
    • Spectroscopic and X-ray crystallographic characterization of bestatin bound to the aminopeptidase from Aeromonas (Vibrio) proteolytica
    • C.C. Stamper, D.L. Bienvenue, B. Bennett, D. Ringe, G.A. Petsko, and R.C. Holz Spectroscopic and X-ray crystallographic characterization of bestatin bound to the aminopeptidase from Aeromonas (Vibrio) proteolytica Biochemistry 43 2004 9620 9628
    • (2004) Biochemistry , vol.43 , pp. 9620-9628
    • Stamper, C.C.1    Bienvenue, D.L.2    Bennett, B.3    Ringe, D.4    Petsko, G.A.5    Holz, R.C.6
  • 15
    • 0036691521 scopus 로고    scopus 로고
    • The 1.20 Å resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with Tris: A tale of buffer inhibition
    • W.T. Desmarais, D.L. Bienvenue, K.P. Bzymek, R.C. Holz, G.A. Petsko, and D. Ringe The 1.20 Å resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with Tris: a tale of buffer inhibition Structure 8 2002 1063 1072
    • (2002) Structure , vol.8 , 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
  • 16
    • 3843081911 scopus 로고    scopus 로고
    • The catalytic role of glutamate 151 in the leucine aminopeptidase from Aeromonas proteolytica
    • K.P. Bzymek, and R.C. Holz The catalytic role of glutamate 151 in the leucine aminopeptidase from Aeromonas proteolytica J. Biol. Chem. 279 2004 31018 31025
    • (2004) J. Biol. Chem. , vol.279 , pp. 31018-31025
    • Bzymek, K.P.1    Holz, R.C.2
  • 17
    • 3342995026 scopus 로고    scopus 로고
    • Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus
    • Y. Fundoiano-Hershcovitz, L. Rabinovitch, Y. Langut, V. Reiland, G. Shoham, and Y. Shoham Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus FEBS. Lett. 571 2004 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
  • 18
    • 0015803160 scopus 로고
    • The proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). Purification and characterization of the aminopeptidases
    • K.D. Vosbeck, K.F. Chow, and W.M. Awad Jr. The proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). Purification and characterization of the aminopeptidases J. Biol. Chem. 248 1973 6029 6034
    • (1973) J. Biol. Chem. , vol.248 , pp. 6029-6034
    • Vosbeck, K.D.1    Chow, K.F.2    Awad Jr., W.M.3
  • 19
    • 0016823634 scopus 로고
    • The proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). Specificity and immobilization of aminopeptidase
    • K.D. Vosbeck, B.D. Greenberg, and W.M. Awad Jr. The proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). Specificity and immobilization of aminopeptidase J. Biol. Chem. 250 1975 3981 3987
    • (1975) J. Biol. Chem. , vol.250 , pp. 3981-3987
    • Vosbeck, K.D.1    Greenberg, B.D.2    Awad Jr., W.M.3
  • 20
    • 0018264520 scopus 로고
    • Proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). Effect of pH, metal ions, and amino acids on aminopeptidase activity
    • K.D. Vosbeck, B.D. Greenberg, M.S. Ochoa, P.L. Whitney, and W.M. Awad Jr. Proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). Effect of pH, metal ions, and amino acids on aminopeptidase activity J. Biol. Chem. 253 1978 257 260
    • (1978) J. Biol. Chem. , vol.253 , pp. 257-260
    • Vosbeck, K.D.1    Greenberg, B.D.2    Ochoa, M.S.3    Whitney, P.L.4    Awad Jr., W.M.5
  • 21
    • 0024334718 scopus 로고
    • Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme
    • A. Spungin, and S. Blumberg Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme Eur. J. Biochem. 183 1989 471 477
    • (1989) Eur. J. Biochem. , vol.183 , pp. 471-477
    • Spungin, A.1    Blumberg, S.2
  • 22
    • 0027473733 scopus 로고
    • Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution
    • D. Ben-Meir, A. Spungin, R. Ashkenazi, and S. Blumberg Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution Eur. J. Biochem. 212 1993 107 112
    • (1993) Eur. J. Biochem. , vol.212 , pp. 107-112
    • Ben-Meir, D.1    Spungin, A.2    Ashkenazi, R.3    Blumberg, S.4
  • 23
    • 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
    • J. Arima, M. Iwabuchi, and T. Hatanaka 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 2004 531 538
    • (2004) Biochem. Biophys. Res. Commun. , vol.317 , pp. 531-538
    • Arima, J.1    Iwabuchi, M.2    Hatanaka, T.3
  • 24
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • C. Yanisch-Perron, J. Vieira, and J. Messing Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors Gene 33 1985 103 119
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 25
    • 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
    • N. Mishima, K. Mizumoto, Y. Iwasaki, H. Nakano, and T. Yamane 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 1997 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
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 15 1970 680 685
    • (1970) Nature , vol.15 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 31444450427 scopus 로고    scopus 로고
    • Alteration of leucine aminopeptidase from Streptomyces septatus TH-2 to phenylalanine aminopeptidase by site-directed mutagenesis
    • J. Arima, Y. Uesugi, M. Iwabuchi, and T. Hatanaka Alteration of leucine aminopeptidase from Streptomyces septatus TH-2 to phenylalanine aminopeptidase by site-directed mutagenesis Appl. Environ. Microbiol. 71 2005 7229 7235
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 7229-7235
    • Arima, J.1    Uesugi, Y.2    Iwabuchi, M.3    Hatanaka, T.4
  • 29
    • 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
    • (in press).
    • Arima, J., Uesugi, Y., Uraji, M., Yatsushiro, S., Tsuboi, S., Iwabuchi, M. and Hatanaka, T. (2006) Modulation of Streptomyces leucine aminopeptidase by calcium: identification and functional analysis of key residues in activation and stabilization by calcium. J. Biol. Chem. (in press).
    • (2006) J. Biol. Chem.
    • Arima, J.1    Uesugi, Y.2    Uraji, M.3    Yatsushiro, S.4    Tsuboi, S.5    Iwabuchi, M.6    Hatanaka, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.