메뉴 건너뛰기




Volumn 55, Issue , 2014, Pages 7-13

Unveiling aminopeptidase P from Streptomyces lavendulae: Molecular cloning, expression and biochemical characterization

Author keywords

Aminopeptidase P; Bradykinin; Gly Pro pNA; Metalloenzyme; Proline aminopeptidase; Streptomyces lavendulae

Indexed keywords

AMINO ACIDS; CLONING; ESCHERICHIA COLI; MANGANESE; METAL IONS; PEPTIDES;

EID: 84891771940     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2013.11.003     Document Type: Article
Times cited : (9)

References (29)
  • 2
    • 68449099281 scopus 로고    scopus 로고
    • Aminopeptidases
    • [Chapter 15], J. Polaina, A.P. MacCabe (Eds.)
    • Sanz Y. Aminopeptidases. Industrial enzymes 2007, 243-260. [Chapter 15]. J. Polaina, A.P. MacCabe (Eds.).
    • (2007) Industrial enzymes , pp. 243-260
    • Sanz, Y.1
  • 3
    • 0028522467 scopus 로고
    • Purification and characterization of a general aminopeptidase from Streptococcus salivarius ssp. thermophilus CNRZ 302
    • Rul F., Monnet V., Gripon J.C. Purification and characterization of a general aminopeptidase from Streptococcus salivarius ssp. thermophilus CNRZ 302. J Dairy Sci 1994, 77:2880-2889.
    • (1994) J Dairy Sci , vol.77 , pp. 2880-2889
    • Rul, F.1    Monnet, V.2    Gripon, J.C.3
  • 4
    • 0033135139 scopus 로고    scopus 로고
    • Purification and characterization of a lysine-p-nitroanilide hydrolase, a broad specificity aminopeptidase, from the cytoplasm of Lactococcus lactis subsp. cremoris AM2
    • McDonnell M., Bouchier P., Fitzgerald R.J., O'Cuinn G. Purification and characterization of a lysine-p-nitroanilide hydrolase, a broad specificity aminopeptidase, from the cytoplasm of Lactococcus lactis subsp. cremoris AM2. J Dairy Res 1999, 66:257-270.
    • (1999) J Dairy Res , vol.66 , pp. 257-270
    • McDonnell, M.1    Bouchier, P.2    Fitzgerald, R.J.3    O'Cuinn, G.4
  • 5
    • 33645700889 scopus 로고    scopus 로고
    • Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica
    • Arima J., Uesugi Y., Iwabuchi M., Hatanaka T. Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica. Appl Microbiol Biotechnol 2006, 70:541-547.
    • (2006) Appl Microbiol Biotechnol , vol.70 , pp. 541-547
    • Arima, J.1    Uesugi, Y.2    Iwabuchi, M.3    Hatanaka, T.4
  • 6
    • 0001138738 scopus 로고
    • Bitter flavour in dairy products. II. A review of bitter peptides from caseins: their formation, isolation and identification, structure masking and inhibition
    • Lemieux L., Simard R.E. Bitter flavour in dairy products. II. A review of bitter peptides from caseins: their formation, isolation and identification, structure masking and inhibition. Lait 1991, 72:335-382.
    • (1991) Lait , vol.72 , pp. 335-382
    • Lemieux, L.1    Simard, R.E.2
  • 8
    • 19944432008 scopus 로고    scopus 로고
    • Human recombinant membrane-bound aminopeptidase P: production of a soluble form and characterization using novel internally quenched fluorescent substrates
    • Molinaro G., Carmona A.K., Juliano M.A., Juliano L., Malitskaya E., Yessine M.A., et al. Human recombinant membrane-bound aminopeptidase P: production of a soluble form and characterization using novel internally quenched fluorescent substrates. J Biochem 2005, 385:389-397.
    • (2005) J Biochem , vol.385 , pp. 389-397
    • Molinaro, G.1    Carmona, A.K.2    Juliano, M.A.3    Juliano, L.4    Malitskaya, E.5    Yessine, M.A.6
  • 9
    • 38349111478 scopus 로고    scopus 로고
    • Streptomyces aminopeptidase P: biochemical characterization and insight into the roles of its N-terminal domain
    • Arima J., Uesugi Y., Iwabuchi M., Hatanaka T. Streptomyces aminopeptidase P: biochemical characterization and insight into the roles of its N-terminal domain. Protein Eng Des Sel 2008, 21:45-53.
    • (2008) Protein Eng Des Sel , vol.21 , pp. 45-53
    • Arima, J.1    Uesugi, Y.2    Iwabuchi, M.3    Hatanaka, T.4
  • 10
    • 1842531108 scopus 로고    scopus 로고
    • Gene cloning and overproduction of an aminopeptidase from Streptomyces septatus TH-2, and comparison with calcium activated enzyme from Streptomyces griseus
    • Arima J., Iwabuchi M., Hatanaka T. Gene cloning and overproduction of an aminopeptidase from Streptomyces septatus TH-2, and comparison with calcium activated enzyme from Streptomyces griseus. Biochem Biophys Res Commun 2004, 317:531-538.
    • (2004) Biochem Biophys Res Commun , vol.317 , pp. 531-538
    • Arima, J.1    Iwabuchi, M.2    Hatanaka, T.3
  • 11
    • 79952709072 scopus 로고    scopus 로고
    • Proline specific aminopeptidase purified from Streptomyces lavendulae
    • Nandan A., Pandey A., Nampoothiri K.M. Proline specific aminopeptidase purified from Streptomyces lavendulae. Appl Biochem Biotechnol 2011, 163:994-1001.
    • (2011) Appl Biochem Biotechnol , vol.163 , pp. 994-1001
    • Nandan, A.1    Pandey, A.2    Nampoothiri, K.M.3
  • 12
    • 0031774327 scopus 로고    scopus 로고
    • Simple and efficient protocol for isolation of high molecular weight DNA from Streptomyces aureofaciens
    • Tripathi G., Rawal S.K. Simple and efficient protocol for isolation of high molecular weight DNA from Streptomyces aureofaciens. Biotechnol Tech 1998, 12:629-631.
    • (1998) Biotechnol Tech , vol.12 , pp. 629-631
    • Tripathi, G.1    Rawal, S.K.2
  • 14
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • Lowry O., Rosebrough N., Farr A., Randall R. Protein measurement with the Folin phenol reagent. J Biol Chem 1951, 193:251.
    • (1951) J Biol Chem , vol.193 , pp. 251
    • Lowry, O.1    Rosebrough, N.2    Farr, A.3    Randall, R.4
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0023774678 scopus 로고
    • Novel assay method for aminopeptidase P and partial purification of two types of the enzyme in Escherichia coli
    • Yoshimoto T., Murayama N., Tsuru D. Novel assay method for aminopeptidase P and partial purification of two types of the enzyme in Escherichia coli. Agric Biol Chem 1988, 52:1957-1963.
    • (1988) Agric Biol Chem , vol.52 , pp. 1957-1963
    • Yoshimoto, T.1    Murayama, N.2    Tsuru, D.3
  • 17
    • 18944408292 scopus 로고    scopus 로고
    • Characterization of two new aminopeptidases in Escherichia coli
    • Zheng Y., Roberts R.J., Kasif S., Guan C. Characterization of two new aminopeptidases in Escherichia coli. J Bacteriol 2005, 187:3671-3677.
    • (2005) J Bacteriol , vol.187 , pp. 3671-3677
    • Zheng, Y.1    Roberts, R.J.2    Kasif, S.3    Guan, C.4
  • 18
    • 0027464168 scopus 로고
    • Cloning and characterization of an aminopeptidase P-encoding gene from Streptomyces lividans
    • Butler M.J., Bergeron A., Soostmeyer G., Zimny T., Malek L.T. Cloning and characterization of an aminopeptidase P-encoding gene from Streptomyces lividans. Gene 1993, 123:115-119.
    • (1993) Gene , vol.123 , pp. 115-119
    • Butler, M.J.1    Bergeron, A.2    Soostmeyer, G.3    Zimny, T.4    Malek, L.T.5
  • 19
    • 0034642182 scopus 로고    scopus 로고
    • Cloning expression, and characterization of human cytosolic aminopeptidase P: a single manganese (II)-dependent enzyme
    • Cottrell G.S., Hooper N.M., Turner A.J. Cloning expression, and characterization of human cytosolic aminopeptidase P: a single manganese (II)-dependent enzyme. Biochemistry 2000, 39:15121-15128.
    • (2000) Biochemistry , vol.39 , pp. 15121-15128
    • Cottrell, G.S.1    Hooper, N.M.2    Turner, A.J.3
  • 21
    • 32344440010 scopus 로고    scopus 로고
    • Tyrosine 387 and arginine 404 are critical in the hydrolytic mechanism of Escherichia coli aminopeptidase P
    • Jao S.C., Huang L.F., Hwang S.M., Li W.S. Tyrosine 387 and arginine 404 are critical in the hydrolytic mechanism of Escherichia coli aminopeptidase P. J Biochem 2006, 45:1547-1553.
    • (2006) J Biochem , vol.45 , pp. 1547-1553
    • Jao, S.C.1    Huang, L.F.2    Hwang, S.M.3    Li, W.S.4
  • 22
    • 33644947161 scopus 로고    scopus 로고
    • Cloning expression, and characterization of aminopeptidase P from the hyperthermophilic archaeon Thermococcus sp. strain NA1
    • Lee H.S., Kim Y.J., Bae S.S., Jeon J.H., Lim J.K., Jeong B.C., et al. Cloning expression, and characterization of aminopeptidase P from the hyperthermophilic archaeon Thermococcus sp. strain NA1. Appl Environ Microbiol 2006, 72:1886-1890.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 1886-1890
    • Lee, H.S.1    Kim, Y.J.2    Bae, S.S.3    Jeon, J.H.4    Lim, J.K.5    Jeong, B.C.6
  • 23
    • 0026701332 scopus 로고
    • Membrane-bound aminopeptidase P from bovine lung. Its purification, properties, and degradation of bradykinin
    • Simmons W.H., Orawski A.T. Membrane-bound aminopeptidase P from bovine lung. Its purification, properties, and degradation of bradykinin. J Biol Chem 1992, 267:4897-4903.
    • (1992) J Biol Chem , vol.267 , pp. 4897-4903
    • Simmons, W.H.1    Orawski, A.T.2
  • 24
    • 37349084922 scopus 로고    scopus 로고
    • Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu
    • Graham S.C., Guss J.M. Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu. Arch Biochem Biophys 2008, 469:200-208.
    • (2008) Arch Biochem Biophys , vol.469 , pp. 200-208
    • Graham, S.C.1    Guss, J.M.2
  • 25
    • 0031201035 scopus 로고    scopus 로고
    • Purification and characterization of aminopeptidase P from Lactococcus lactis subsp. cremoris
    • McDonnell M., Fitzerald R., Fhaolain I., Jennings P.V., O'Cuinn G. Purification and characterization of aminopeptidase P from Lactococcus lactis subsp. cremoris. J Dairy Res 1997, 64:399-407.
    • (1997) J Dairy Res , vol.64 , pp. 399-407
    • McDonnell, M.1    Fitzerald, R.2    Fhaolain, I.3    Jennings, P.V.4    O'Cuinn, G.5
  • 26
    • 13144259676 scopus 로고    scopus 로고
    • Metal-binding and active-site structure of di-zinc Streptomyces griseus aminopeptidase
    • Lin L.Y., Park H.I., Ming L.J. Metal-binding and active-site structure of di-zinc Streptomyces griseus aminopeptidase. J Biol Inorg Chem 1997, 2:744-749.
    • (1997) J Biol Inorg Chem , vol.2 , pp. 744-749
    • Lin, L.Y.1    Park, H.I.2    Ming, L.J.3
  • 27
    • 0023777507 scopus 로고
    • Cloning and expression of aminopeptidase P gene from Escherichia coli HB101 and characterization of expressed enzyme
    • Yoshimoto T., Murayama N., Honda T., Tone H., Tsuru D. Cloning and expression of aminopeptidase P gene from Escherichia coli HB101 and characterization of expressed enzyme. J Biochem 1988, 104:93-97.
    • (1988) J Biochem , vol.104 , pp. 93-97
    • Yoshimoto, T.1    Murayama, N.2    Honda, T.3    Tone, H.4    Tsuru, D.5
  • 28
    • 0028198617 scopus 로고
    • Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold
    • Bazan J.F., Weaver L.H., Roderick S.L., Huber R., Matthews B.W. Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold. Proc Natl Acad Sci U S A 1994, 91:2473-2477.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 2473-2477
    • Bazan, J.F.1    Weaver, L.H.2    Roderick, S.L.3    Huber, R.4    Matthews, B.W.5
  • 29
    • 16644366514 scopus 로고    scopus 로고
    • Structure of Escherichia coli aminopeptidase P in complex with the inhibitor apstatin
    • Graham S.C., Maher M.J., Simmons W.H., Freeman H.C., Guss J.M. Structure of Escherichia coli aminopeptidase P in complex with the inhibitor apstatin. Acta Crystallogr 2004, 60:1770-1779.
    • (2004) Acta Crystallogr , vol.60 , pp. 1770-1779
    • Graham, S.C.1    Maher, M.J.2    Simmons, W.H.3    Freeman, H.C.4    Guss, J.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.