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Volumn 270, Issue 14, 2003, Pages 3074-3082

Characterization of a functionally expressed dipeptidyl aminopeptidase III from Drosophila melanogaster

Author keywords

Enkephalinase; Genome sequencing; Insects; Neuropeptides; Proctolin

Indexed keywords

DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; DIPEPTIDYL PEPTIDASE; DIPEPTIDYL PEPTIDASE III; NEUROPEPTIDE; PROCTOLIN; TYNORPHIN; UNCLASSIFIED DRUG;

EID: 0038713607     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03689.x     Document Type: Article
Times cited : (27)

References (23)
  • 1
    • 0014217151 scopus 로고
    • Dipeptidyl arylamidase III of the pituitary
    • Ellis, S. & Nuenke, J.M. (1967) Dipeptidyl arylamidase III of the pituitary. J. Biol. Chem. 243, 4623-4629.
    • (1967) J. Biol. Chem. , vol.243 , pp. 4623-4629
    • Ellis, S.1    Nuenke, J.M.2
  • 2
    • 0032518744 scopus 로고    scopus 로고
    • Dipeptidyl peptidase III is a zinc metalloexopeptidase. Molecular cloning and expression
    • Fukasawa, K., Fukasawa, K.M., Kanai, M., Fujii, S., Hirose, J. & Harada, M. (1998) Dipeptidyl peptidase III is a zinc metalloexopeptidase. Molecular cloning and expression. Biochem. J. 329, 275-282.
    • (1998) Biochem. J. , vol.329 , pp. 275-282
    • Fukasawa, K.1    Fukasawa, K.M.2    Kanai, M.3    Fujii, S.4    Hirose, J.5    Harada, M.6
  • 3
    • 0033384701 scopus 로고    scopus 로고
    • Dipeptidyl peptidase III from rat liver cytosol: Purification, molecular cloning and immunohistochemical localization
    • Ohkubo, I., Li, Y.H., Maeda, T., Yamamoto, Y., Yamane, T., Du, P.G. & Nishi, K. (1999) Dipeptidyl peptidase III from rat liver cytosol: purification, molecular cloning and immunohistochemical localization. Biol. Chem. 380, 1421-1430.
    • (1999) Biol. Chem. , vol.380 , pp. 1421-1430
    • Ohkubo, I.1    Li, Y.H.2    Maeda, T.3    Yamamoto, Y.4    Yamane, T.5    Du, P.G.6    Nishi, K.7
  • 4
    • 0033614807 scopus 로고    scopus 로고
    • The HELLGH motif of rat liver dipeptidyl peptidase III is involved in zinc coordination and the catalytic activity of the enzyme
    • Fukasawa, K., Fukasawa, K.M., Iwamoto, H., Hirose, J. & Harada, M. (1999) The HELLGH motif of rat liver dipeptidyl peptidase III is involved in zinc coordination and the catalytic activity of the enzyme. Biochemistry 38, 8299-8303.
    • (1999) Biochemistry , vol.38 , pp. 8299-8303
    • Fukasawa, K.1    Fukasawa, K.M.2    Iwamoto, H.3    Hirose, J.4    Harada, M.5
  • 5
    • 0028180056 scopus 로고
    • Dipeptidyl aminopeptidase activities of guinea-pig brain
    • Smyth, M. & O'Cuinn, G. (1994) Dipeptidyl aminopeptidase activities of guinea-pig brain. Int. J. Biochem. 26, 913-921.
    • (1994) Int. J. Biochem. , vol.26 , pp. 913-921
    • Smyth, M.1    O'Cuinn, G.2
  • 6
    • 0028962492 scopus 로고
    • Properties of rat brain dipeptidyl aminopeptidases in the presence of detergents
    • Alba, F., Arenas, J.C. & Lopez, M.A. (1995) Properties of rat brain dipeptidyl aminopeptidases in the presence of detergents. Peptides 16, 325-329.
    • (1995) Peptides , vol.16 , pp. 325-329
    • Alba, F.1    Arenas, J.C.2    Lopez, M.A.3
  • 7
    • 0020465332 scopus 로고
    • Dipeptidyl-aminopeptidase III of rat brain selective affinity for enkephalin and angiotensin
    • Lee, C.-M. & Snyder, S.H. (1982) Dipeptidyl-aminopeptidase III of rat brain selective affinity for enkephalin and angiotensin. J. Biol. Chem. 257, 12043-12050.
    • (1982) J. Biol. Chem. , vol.257 , pp. 12043-12050
    • Lee, C.-M.1    Snyder, S.H.2
  • 8
    • 0023655385 scopus 로고
    • Proctolin degradation by membrane peptidases from nervous tissues of the desert locust Schistocerca gregaria
    • Isaac, R.E. (1987) Proctolin degradation by membrane peptidases from nervous tissues of the desert locust Schistocerca gregaria. Biochem. J. 245, 365-370.
    • (1987) Biochem. J. , vol.245 , pp. 365-370
    • Isaac, R.E.1
  • 9
    • 84990437067 scopus 로고
    • Degradation of the neuropeptide proctolin by membrane bound proteases of the hindgut and ovary of Locusta migratoria and the effects of different inhibitors
    • Puiroux, J. & Loughton, B.G. (1992a) Degradation of the neuropeptide proctolin by membrane bound proteases of the hindgut and ovary of Locusta migratoria and the effects of different inhibitors. Arch. Insect Biochem. Physiol. 19, 193-202.
    • (1992) Arch. Insect Biochem. Physiol. , vol.19 , pp. 193-202
    • Puiroux, J.1    Loughton, B.G.2
  • 11
    • 0001665580 scopus 로고
    • In vitro inactivation of the insect neuropeptide proctolin in haemolymph from Periplaneta americana
    • Steele, R.W. & Starratt, A.N. (1985) In vitro inactivation of the insect neuropeptide proctolin in haemolymph from Periplaneta americana. Insect Biochem. 15, 511-519.
    • (1985) Insect Biochem. , vol.15 , pp. 511-519
    • Steele, R.W.1    Starratt, A.N.2
  • 12
    • 0034786401 scopus 로고    scopus 로고
    • Purification, partial sequencing and characterization of an insect membrane dipeptidyl aminopeptidase that degrades the insect neuropeptide proctolin
    • Mazzocco, C., Fukasawa, K.M., Raymond, A.A. & Puiroux, J. (2001) Purification, partial sequencing and characterization of an insect membrane dipeptidyl aminopeptidase that degrades the insect neuropeptide proctolin. Eur J. Biochem. 268, 4940-4949.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4940-4949
    • Mazzocco, C.1    Fukasawa, K.M.2    Raymond, A.A.3    Puiroux, J.4
  • 14
    • 0034054393 scopus 로고    scopus 로고
    • Purification of proctolin-binding protein from the foregut of the insect Blaberus craniifer
    • Mazzocco, C. & Puiroux, J. (2000) Purification of proctolin-binding protein from the foregut of the insect Blaberus craniifer. Eur. J. Biochem. 267, 2252-2259.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2252-2259
    • Mazzocco, C.1    Puiroux, J.2
  • 15
    • 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
  • 16
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. & Doolittle, R.F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 0034111712 scopus 로고    scopus 로고
    • Characterization of tynorphin, a potent endogenous inhibitor of dipeptidyl peptidase III
    • Yamamoto, Y., Hashimoto, J., Shimamura, M., Yamaguchi, T. & Hazato, T. (2000) Characterization of tynorphin, a potent endogenous inhibitor of dipeptidyl peptidase III. Peptides 21, 503-508.
    • (2000) Peptides , vol.21 , pp. 503-508
    • Yamamoto, Y.1    Hashimoto, J.2    Shimamura, M.3    Yamaguchi, T.4    Hazato, T.5
  • 20
    • 0024267199 scopus 로고
    • Human placental dipeptidyl aminopeptidase III: Hydrolysis of enkephalins and its stimulation by cobaltous ion
    • Shimamori, Y., Watanabe, Y. & Fujimoto, Y. (1988) Human placental dipeptidyl aminopeptidase III: hydrolysis of enkephalins and its stimulation by cobaltous ion. Biochem. Med. Metab Biol. 40, 305-310.
    • (1988) Biochem. Med. Metab. Biol. , vol.40 , pp. 305-310
    • Shimamori, Y.1    Watanabe, Y.2    Fujimoto, Y.3
  • 21
    • 0023740569 scopus 로고
    • Dipeptidyl peptidase III and alanyl aminopeptidase in the human seminal plasma: Origin and biochemical properties
    • Vanha-Perttula, T. (1988) Dipeptidyl peptidase III and alanyl aminopeptidase in the human seminal plasma: origin and biochemical properties. Clin. Chim Acta. 177, 179-195.
    • (1988) Clin. Chim. Acta , vol.177 , pp. 179-195
    • Vanha-Perttula, T.1
  • 22
    • 0342572537 scopus 로고    scopus 로고
    • Molecular cloning and immunohistochemical localization of rat dipeptidyl peptidase III
    • Ohkubo, I., Li, Y., Maeda, T., Yamamoto, Y., Yamane, T., Du, P.G. & Nishi, K. (2000) Molecular cloning and immunohistochemical localization of rat dipeptidyl peptidase III. Forensic Sci. Int. 113, 147-151.
    • (2000) Forensic. Sci. Int. , vol.113 , pp. 147-151
    • Ohkubo, I.1    Li, Y.2    Maeda, T.3    Yamamoto, Y.4    Yamane, T.5    Du, P.G.6    Nishi, K.7
  • 23
    • 0034352286 scopus 로고    scopus 로고
    • Human and rat dipeptidyl peptidase III: Biochemical and mass spectrometric arguments for similarities and differences
    • Abramic, M., Schleuder, D., Dolovcak, L., Schroder, W., Strupat, K., Sagi, D., Peter-Katalini, J. & Vitale, L. (2000) Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric arguments for similarities and differences. Biol. Chem. 381, 1233-1243.
    • (2000) Biol. Chem. , vol.381 , pp. 1233-1243
    • Abramic, M.1    Schleuder, D.2    Dolovcak, L.3    Schroder, W.4    Strupat, K.5    Sagi, D.6    Peter-Katalini, J.7    Vitale, L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.