메뉴 건너뛰기




Volumn 16, Issue 3, 2000, Pages 219-229

Aminopeptidase yscCo-II: A new cobalt-dependent aminopeptidase from yeast - Purification and biochemical characterization

Author keywords

Cobalt dependent aminopeptidase; Protease; Protein degradation; Saccharomyces cerevisiae

Indexed keywords

1,10 PHENANTHROLINE; AMINOPEPTIDASE; BESTATIN; COBALT; ENZYME INHIBITOR; PROTEINASE INHIBITOR;

EID: 0033975579     PISSN: 0749503X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0061(200002)16:3<219::AID-YEA523>3.0.CO;2-J     Document Type: Article
Times cited : (16)

References (41)
  • 2
    • 0022277838 scopus 로고
    • Proteinases, protcolysis and biological control in the yeast Sacrharomyces cerevisiae
    • Achstetter T, Wolf DH. 1985. Proteinases, protcolysis and biological control in the yeast Sacrharomyces cerevisiae. Yeast 1: 139-157.
    • (1985) Yeast , vol.1 , pp. 139-157
    • Achstetter, T.1    Wolf, D.H.2
  • 4
    • 0028951721 scopus 로고
    • Cis and transacting regulatory elements required for regulation of the CPS1 gene in Saccharomyces cerevisiae
    • Bordallo J, Suárez-Rendueles MP. 1995. Cis and transacting regulatory elements required for regulation of the CPS1 gene in Saccharomyces cerevisiae. Mol Gen Genet 246: 580-589.
    • (1995) Mol Gen Genet , vol.246 , pp. 580-589
    • Bordallo, J.1    Suárez-Rendueles, M.P.2
  • 5
    • 0028911096 scopus 로고
    • Transcriptional regulation of the yeast vacuolar aminopeptidase yscl encoding gene (APE1) by carbon sources
    • Bordallo J, Cueva R, Suárez-Rendueles MP. 1995. Transcriptional regulation of the yeast vacuolar aminopeptidase yscl encoding gene (APE1) by carbon sources. FEBS Lett 364: 13-16.
    • (1995) FEBS Lett , vol.364 , pp. 13-16
    • Bordallo, J.1    Cueva, R.2    Suárez-Rendueles, M.P.3
  • 6
    • 0025251693 scopus 로고
    • Purification and characterization of a methionine aminopeptidase from Saccharomyces cerevisiae
    • Chang YH, Teichert U, Smith JA. 1990. Purification and characterization of a methionine aminopeptidase from Saccharomyces cerevisiae. J Biol Chem 265: 19892-19897.
    • (1990) J Biol Chem , vol.265 , pp. 19892-19897
    • Chang, Y.H.1    Teichert, U.2    Smith, J.A.3
  • 7
    • 0024788273 scopus 로고
    • Yeast vacuolar aminopeptidase yscI. Isolation and regulation of the APE1 (LAP4) structural gene
    • Cuevas R, Garcia-Alvarez N, Suárez-Rendueles MP. 1989. Yeast vacuolar aminopeptidase yscI. Isolation and regulation of the APE1 (LAP4) structural gene. FEBS Lett 259: 125-129.
    • (1989) FEBS Lett , vol.259 , pp. 125-129
    • Cuevas, R.1    Garcia-Alvarez, N.2    Suárez-Rendueles, M.P.3
  • 9
    • 0027499191 scopus 로고
    • BLH1 codes for a yeast aminopeptidase, the equivalent of mammalian bleomycin hydrolase
    • Enenkel C, Wolf DH. 1993. BLH1 codes for a yeast aminopeptidase, the equivalent of mammalian bleomycin hydrolase. J Biol Chem 268: 7036-7043.
    • (1993) J Biol Chem , vol.268 , pp. 7036-7043
    • Enenkel, C.1    Wolf, D.H.2
  • 10
    • 0018183217 scopus 로고
    • Subcellular localization and levels of aminopeptidases and dipeptidases in Saccharomyces cerevisiae
    • Frey J, Röhm KH. 1978. Subcellular localization and levels of aminopeptidases and dipeptidases in Saccharomyces cerevisiae. Biochim Biophys Acta 527: 31-41.
    • (1978) Biochim Biophys Acta , vol.527 , pp. 31-41
    • Frey, J.1    Röhm, K.H.2
  • 13
    • 0023838558 scopus 로고
    • Enzymes required for yeast prohormone processing
    • Fuller RS, Sterne RE, Thorner J. 1988. Enzymes required for yeast prohormone processing. Ann Rev Physiol 50: 345-368.
    • (1988) Ann Rev Physiol , vol.50 , pp. 345-368
    • Fuller, R.S.1    Sterne, R.E.2    Thorner, J.3
  • 14
    • 0026343673 scopus 로고
    • Molecular cloning of soluble aminopeptidases from Saccharomyces cerevisiae. Sequence analysis of aminopeptidase yscII, a putative zinc-metallopeptidase
    • Garcia-Alvarez N, Cueva R, Suárez-Rendueles MP. 1991. Molecular cloning of soluble aminopeptidases from Saccharomyces cerevisiae. Sequence analysis of aminopeptidase yscII, a putative zinc-metallopeptidase. Eur J Biochem 202: 993-1002.
    • (1991) Eur J Biochem , vol.202 , pp. 993-1002
    • Garcia-Alvarez, N.1    Cueva, R.2    Suárez-Rendueles, M.P.3
  • 15
    • 0032525130 scopus 로고    scopus 로고
    • Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae
    • Gilon T, Chomsky O, Kulka RG. 1998. Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae. EMBO J 17: 2759-2766.
    • (1998) EMBO J , vol.17 , pp. 2759-2766
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 17
    • 0025980627 scopus 로고
    • Proteinase yscE, the yeast proteosome/multicatalytic proteinase: Mutants unravel its necessity for cell survival
    • Heinemeyer W, Kleinschmidt JA, Saidowsky J, Escher C, Wolf DH. 1991. Proteinase yscE, the yeast proteosome/multicatalytic proteinase: mutants unravel its necessity for cell survival. EMBO J 10: 555-562.
    • (1991) EMBO J , vol.10 , pp. 555-562
    • Heinemeyer, W.1    Kleinschmidt, J.A.2    Saidowsky, J.3    Escher, C.4    Wolf, D.H.5
  • 19
    • 0038651316 scopus 로고
    • Yeast Saccharomyces cerevisiae proteinases: Structure, characteristics and function
    • Walton EF, Yarranton GT (eds). Blackie: London
    • Hirsch HH, Suárez-Rendueles P, Wolf DH. 1989. Yeast Saccharomyces cerevisiae proteinases: structure, characteristics and function. In Molecular and Cell Biology of Yeasts, Walton EF, Yarranton GT (eds). Blackie: London; 134-200.
    • (1989) Molecular and Cell Biology of Yeasts , pp. 134-200
    • Hirsch, H.H.1    Suárez-Rendueles, P.2    Wolf, D.H.3
  • 20
    • 0019887627 scopus 로고
    • Binding of hydroxamic acid inhibitors to crystalline thermolysin suggest a pentacoordinate zinc intermediate in catalysis
    • Holmes MA, Matthcus BW. 1981. Binding of hydroxamic acid inhibitors to crystalline thermolysin suggest a pentacoordinate zinc intermediate in catalysis. Biochemistry 20: 6912-6921.
    • (1981) Biochemistry , vol.20 , pp. 6912-6921
    • Holmes, M.A.1    Matthcus, B.W.2
  • 21
    • 0032539578 scopus 로고    scopus 로고
    • The structural aspects of limited protcolysis of native proteins
    • Hubbard SJ. 1998. The structural aspects of limited protcolysis of native proteins. Biochem Biophys Acta 1382: 191-206.
    • (1998) Biochem Biophys Acta , vol.1382 , pp. 191-206
    • Hubbard, S.J.1
  • 22
    • 0025871691 scopus 로고
    • Three proteolytic systems in the yeast Saccharomyces cerevisiae
    • Jones EE. 1991. Three proteolytic systems in the yeast Saccharomyces cerevisiae. J Biol Chem 266: 7963-7966.
    • (1991) J Biol Chem , vol.266 , pp. 7963-7966
    • Jones, E.E.1
  • 23
    • 0032079372 scopus 로고    scopus 로고
    • Non-classical protein sorting to the yeast vacuole
    • Klionsky DJ. 1998. Non-classical protein sorting to the yeast vacuole. J Biol Chem 273: 10807-10810.
    • (1998) J Biol Chem , vol.273 , pp. 10807-10810
    • Klionsky, D.J.1
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0000870917 scopus 로고    scopus 로고
    • Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Succharomyces cerevisiae
    • Lee DH, Goldberg AL. 1996. Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Succharomyces cerevisiae. J Biol Chem 271: 27280-27284.
    • (1996) J Biol Chem , vol.271 , pp. 27280-27284
    • Lee, D.H.1    Goldberg, A.L.2
  • 26
    • 0017127519 scopus 로고
    • Yeast aminopeptidase I. Chemical composition and catalytic properties
    • Metz G, Röhm KH. 1976. Yeast aminopeptidase I. Chemical composition and catalytic properties. Biochem Biophys Acta 429: 933-949.
    • (1976) Biochem Biophys Acta , vol.429 , pp. 933-949
    • Metz, G.1    Röhm, K.H.2
  • 27
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • Morrisey JH. 1981. Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal Biochem 17: 307-310.
    • (1981) Anal Biochem , vol.17 , pp. 307-310
    • Morrisey, J.H.1
  • 28
    • 0028304451 scopus 로고
    • Molecular cloning of the aminopeptidase Y gene of Saccharomyces cerevisiae
    • Nishizawa M, Yasuhara T, Nakai T, Fujiki Y, Ohashi A. 1994. Molecular cloning of the aminopeptidase Y gene of Saccharomyces cerevisiae. J Biol Chem 269: 13651-13655.
    • (1994) J Biol Chem , vol.269 , pp. 13651-13655
    • Nishizawa, M.1    Yasuhara, T.2    Nakai, T.3    Fujiki, Y.4    Ohashi, A.5
  • 29
    • 0028132691 scopus 로고
    • Proteasomes: Protein degradation machines of the cell
    • Peters JM. 1994. Proteasomes: protein degradation machines of the cell. Trends Biochem Soc 19: 377-382.
    • (1994) Trends Biochem Soc , vol.19 , pp. 377-382
    • Peters, J.M.1
  • 30
  • 31
    • 0027516156 scopus 로고
    • Proteosomes: Multicatalytic proteinase complexes
    • Rivett AJ. 1993. Proteosomes: multicatalytic proteinase complexes. Biochem J 291: 1-10.
    • (1993) Biochem J , vol.291 , pp. 1-10
    • Rivett, A.J.1
  • 32
    • 0027273988 scopus 로고
    • Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: A new type of proteolytic enzyme
    • Roderick SL, Matthews BW. 1993. Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme. Biochemistry 32: 3907-3912.
    • (1993) Biochemistry , vol.32 , pp. 3907-3912
    • Roderick, S.L.1    Matthews, B.W.2
  • 33
    • 0002006941 scopus 로고
    • Inhibition of proteolytic enzymes
    • Beynon RJ, Bond JS (eds). IRL Press: Oxford
    • Salvesen G, Nagase H. 1989. Inhibition of proteolytic enzymes. In Proteolytic Enzymes, Beynon RJ, Bond JS (eds). IRL Press: Oxford; 83-104.
    • (1989) Proteolytic Enzymes , pp. 83-104
    • Salvesen, G.1    Nagase, H.2
  • 34
    • 0017390556 scopus 로고
    • A rapid sensitive and versatile for protein using Coomassie Brilliant Blue G-250
    • Sedmak JJ, Grossberg SE. 1977. A rapid sensitive and versatile for protein using Coomassie Brilliant Blue G-250. Anal Biochem 79: 544-552.
    • (1977) Anal Biochem , vol.79 , pp. 544-552
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 35
    • 0004661509 scopus 로고
    • A new X-prolyl-dipeptidyl amino-peptidase from yeast associated with a particulate fraction
    • Suárez-Rendueles MP, Schwencke J, Garcia-Alvarez N, Gascon S. 1981. A new X-prolyl-dipeptidyl amino-peptidase from yeast associated with a particulate fraction. FEBS Lett 131: 296-300.
    • (1981) FEBS Lett , vol.131 , pp. 296-300
    • Suárez-Rendueles, M.P.1    Schwencke, J.2    Garcia-Alvarez, N.3    Gascon, S.4
  • 36
    • 0023815375 scopus 로고
    • Proteinase function in yeast: Biochemical and genetic approaches to a central mechanism of post-translational control in the eukaryotic cell
    • Suárez-Rendueles MP, Wolf DH. 1988. Proteinase function in yeast: biochemical and genetic approaches to a central mechanism of post-translational control in the eukaryotic cell. FEMS Microbiol Rev 54: 17-46.
    • (1988) FEMS Microbiol Rev , vol.54 , pp. 17-46
    • Suárez-Rendueles, M.P.1    Wolf, D.H.2
  • 37
    • 0027246245 scopus 로고
    • Purification and characterization of the cystinyl bond cleaving yeast amino-peptidase yscXVI
    • Tisljar U, Wolf DH. 1993. Purification and characterization of the cystinyl bond cleaving yeast amino-peptidase yscXVI. FEBS Lett 322: 191-196.
    • (1993) FEBS Lett , vol.322 , pp. 191-196
    • Tisljar, U.1    Wolf, D.H.2
  • 38
    • 0022400582 scopus 로고
    • The slow tight binding of bestatin and amastatin to aminopeptidases
    • Wilkes HS, Prescott JM. 1985. The slow tight binding of bestatin and amastatin to aminopeptidases. J Biol Chem 260: 13154-13162.
    • (1985) J Biol Chem , vol.260 , pp. 13154-13162
    • Wilkes, H.S.1    Prescott, J.M.2
  • 39
    • 0023664606 scopus 로고
    • Hydroxamate-induced spectral perturbations of cobalt Aeromonas aminopeptidase
    • Wilkes HS, Prescott JM. 1987. Hydroxamate-induced spectral perturbations of cobalt Aeromonas aminopeptidase. J Biol Chem 262: 8621-8625.
    • (1987) J Biol Chem , vol.262 , pp. 8621-8625
    • Wilkes, H.S.1    Prescott, J.M.2
  • 40
    • 0028136279 scopus 로고
    • Yeast bleomycin hydrolase is a DNA-binding cysteine protease
    • Xu HE, Johnston SA. 1994. Yeast bleomycin hydrolase is a DNA-binding cysteine protease. J Biol Chem 269: 21177-21183.
    • (1994) J Biol Chem , vol.269 , pp. 21177-21183
    • Xu, H.E.1    Johnston, S.A.2
  • 41
    • 0028308218 scopus 로고
    • Aminopeptidase Y, a new aminopeptidase from Saccharomyces cerevisiae
    • Yasuhara T, Nakai T, Ohashi A. 1994. Aminopeptidase Y, a new aminopeptidase from Saccharomyces cerevisiae. J Biol Chem 269: 13644-13650.
    • (1994) J Biol Chem , vol.269 , pp. 13644-13650
    • Yasuhara, T.1    Nakai, T.2    Ohashi, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.