메뉴 건너뛰기




Volumn 9, Issue 2, 2000, Pages 353-360

Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase family

Author keywords

Amnesia; Inhibitor design; Oxyanion binding site; Site directed mutagenesis; Steady state kinetic studies; Transition state stabilization

Indexed keywords

COMPLEMENTARY DNA; PROLYL ENDOPEPTIDASE; RECOMBINANT PROTEIN;

EID: 0034003936     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.2.353     Document Type: Article
Times cited : (60)

References (35)
  • 1
    • 0021094368 scopus 로고
    • Transition-state stabilization at the oxyanion binding site of serine and thiol proteinases: Hydrolyses of thiono and oxygen esters
    • Asbóth B, Polgár L. 1983. Transition-state stabilization at the oxyanion binding site of serine and thiol proteinases: hydrolyses of thiono and oxygen esters. Biochemistry 22:117-122.
    • (1983) Biochemistry , vol.22 , pp. 117-122
    • Asbóth, B.1    Polgár, L.2
  • 3
    • 0025076877 scopus 로고
    • Slow tight-binding inhibition of prolyl endopeptidase by benzyloxycarbonyl-prolylprolinal
    • Bakker AV, Jung S, Spencer RW, Vinick FJ, Faraci WS. 1990. Slow tight-binding inhibition of prolyl endopeptidase by benzyloxycarbonyl-prolylprolinal. Biochem J 271:559-562.
    • (1990) Biochem J , vol.271 , pp. 559-562
    • Bakker, A.V.1    Jung, S.2    Spencer, R.W.3    Vinick, F.J.4    Faraci, W.S.5
  • 5
    • 0025370164 scopus 로고
    • Functional interaction among catalytic residues in subtilisin BPN'
    • Carter P, Wells JA. 1990. Functional interaction among catalytic residues in subtilisin BPN'. Proteins Struct Funct Genet 7:335-342.
    • (1990) Proteins Struct Funct Genet , vol.7 , pp. 335-342
    • Carter, P.1    Wells, J.A.2
  • 7
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates of trypsin
    • Erlanger BF. Kokowsky N, Cohen W. 1961. The preparation and properties of two new chromogenic substrates of trypsin. Arch Biochem Biophys 95:271-278.
    • (1961) Arch Biochem Biophys , vol.95 , pp. 271-278
    • Erlanger Bf Kokowsky, N.1    Cohen, W.2
  • 9
    • 0032563162 scopus 로고    scopus 로고
    • Prolyl oligopeptidase: An unusual β-propeller domain regulates proteolysis
    • Fülöp V, Böcskei Z, Polgár L. 1998. Prolyl oligopeptidase: An unusual β-propeller domain regulates proteolysis. Cell 94:161-170.
    • (1998) Cell , vol.94 , pp. 161-170
    • Fülöp, V.1    Böcskei, Z.2    Polgár, L.3
  • 10
    • 0014945734 scopus 로고
    • Structure of crystalline α-chymotrypsin. IV. The structure of indoleacryloyl-α-chymotrypsin and its relevance to the hydrolytic mechanism of the enzyme
    • Henderson R. 1970. Structure of crystalline α-chymotrypsin. IV. The structure of indoleacryloyl-α-chymotrypsin and its relevance to the hydrolytic mechanism of the enzyme. J Mol Biol 54:341-354.
    • (1970) J Mol Biol , vol.54 , pp. 341-354
    • Henderson, R.1
  • 11
    • 0030905008 scopus 로고    scopus 로고
    • Benzyloxy-carhonylprolylprolinal, a transition-state analogue for prolyl oligopeptidase, forms a tetrahedral adduct with catalytic serine, not a reactive cysteine
    • Kahyaoglu A, Hughjoo M, Kraicsovits F, Jordan F, Polgár L. 1997. Benzyloxy-carhonylprolylprolinal, a transition-state analogue for prolyl oligopeptidase, forms a tetrahedral adduct with catalytic serine, not a reactive cysteine. Biochem J 322:8390-843.
    • (1997) Biochem J , vol.322 , pp. 8390-8843
    • Kahyaoglu, A.1    Hughjoo, M.2    Kraicsovits, F.3    Jordan, F.4    Polgár, L.5
  • 12
    • 0017324044 scopus 로고
    • Serine proteases: Structure and mechanism of catalysis
    • Kraut J. 1977. Serine proteases: Structure and mechanism of catalysis. Annu Rev Biochem 46:331-358.
    • (1977) Annu Rev Biochem , vol.46 , pp. 331-358
    • Kraut, J.1
  • 14
    • 0028217535 scopus 로고
    • Lower serum prolyl endopeptidase enzyme activity in major depression: Further evidence that peptidases play a role in the pathophysiology of depression
    • Maes M, Goossens F, Scharpé S, Meltzer HY, D'Hondt P, Cosyns P. 1994. Lower serum prolyl endopeptidase enzyme activity in major depression: Further evidence that peptidases play a role in the pathophysiology of depression. Biol Psychiatry 35:545-552.
    • (1994) Biol Psychiatry , vol.35 , pp. 545-552
    • Maes, M.1    Goossens, F.2    Scharpé, S.3    Meltzer, H.Y.4    D'Hondt, P.5    Cosyns, P.6
  • 15
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison JF, Walsh CT. 1988. The behavior and significance of slow-binding enzyme inhibitors. Adv Enzymol Relat Areas Mol Biol 61:201-301.
    • (1988) Adv Enzymol Relat Areas Mol Biol , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 16
    • 77956795079 scopus 로고
    • Structure and function of serine proteases
    • Polgár L. 1987. Structure and function of serine proteases. New Comp Biochem 16:159-200.
    • (1987) New Comp Biochem , vol.16 , pp. 159-200
    • Polgár, L.1
  • 18
    • 0025762537 scopus 로고
    • PH-Dependent mechanisms in the catalysis of prolyl endopeptidase from pig muscle
    • Polgár L. 1991. pH-Dependent mechanisms in the catalysis of prolyl endopeptidase from pig muscle. Eur J Biochem 197:441-447.
    • (1991) Eur J Biochem , vol.197 , pp. 441-447
    • Polgár, L.1
  • 19
    • 0026669767 scopus 로고
    • Structural relationship between lipases and peptidases of the prolyl oligopeptidase family
    • Polgár L. 1992a. Structural relationship between lipases and peptidases of the prolyl oligopeptidase family. FEBS Lett 311:281-284.
    • (1992) FEBS Lett , vol.311 , pp. 281-284
    • Polgár, L.1
  • 20
    • 0026550666 scopus 로고
    • Prolyl endopeptidase catalysis: A physical rather than a chemical step is rate-limiting
    • Polgár L. 1992b. Prolyl endopeptidase catalysis: A physical rather than a chemical step is rate-limiting. Biochem J 283:647-648.
    • (1992) Biochem J , vol.283 , pp. 647-648
    • Polgár, L.1
  • 21
    • 0028672897 scopus 로고
    • Prolyl oligopeptidases
    • Polgár L. 1994. Prolyl oligopeptidases. Methods Enzymol 244:188-200.
    • (1994) Methods Enzymol , vol.244 , pp. 188-200
    • Polgár, L.1
  • 22
    • 0028826743 scopus 로고
    • Effects of ionic strength on the catalysis and stability of prolyl oligopeptidase
    • Polgár L. 1995. Effects of ionic strength on the catalysis and stability of prolyl oligopeptidase. Biochem J 312:267-271.
    • (1995) Biochem J , vol.312 , pp. 267-271
    • Polgár, L.1
  • 23
    • 33646778206 scopus 로고    scopus 로고
    • Basic kinetic mechanisms of proteolytic enzymes
    • Sterchi EE, Stöcker W, eds. Heidelberg: Springer Verlag
    • Polgár L. 1999. Basic kinetic mechanisms of proteolytic enzymes. In: Sterchi EE, Stöcker W, eds. Laboratory manual on proteolytic enzymes. Heidelberg: Springer Verlag. pp 148-166.
    • (1999) Laboratory Manual on Proteolytic Enzymes , pp. 148-166
    • Polgár, L.1
  • 24
    • 0027309007 scopus 로고
    • Prolyl oligopeptidase catalysis. Reactions with thiono substrates reveal substrate-induced conformational change to be the rate-limiting step
    • Polgár L, Kollát E, Hollósi M. 1993. Prolyl oligopeptidase catalysis. Reactions with thiono substrates reveal substrate-induced conformational change to be the rate-limiting step. FEBS Lett 322:227-230.
    • (1993) FEBS Lett , vol.322 , pp. 227-230
    • Polgár, L.1    Kollát, E.2    Hollósi, M.3
  • 25
    • 0029977323 scopus 로고    scopus 로고
    • New prolyl endopeptidase inhibitors: In vitro and in vivo activities of azabicyclo[2,2,2]octane, azabicyclo[2,2,1]heptane, and perhydroindole derivatives
    • Portevin B, Benoist A, Rémond G, Hervé Y, Vincent M, Lepagnol JD, Nanteuil G. 1996. New prolyl endopeptidase inhibitors: In vitro and in vivo activities of azabicyclo[2,2,2]octane, azabicyclo[2,2,1]heptane, and perhydroindole derivatives. J Med Chem 39:2379-2391.
    • (1996) J Med Chem , vol.39 , pp. 2379-2391
    • Portevin, B.1    Benoist, A.2    Rémond, G.3    Hervé, Y.4    Vincent, M.5    Lepagnol, J.D.6    Nanteuil, G.7
  • 27
    • 0026077358 scopus 로고
    • A new family of serine-type peptidases related to prolyl oligopeptidase
    • Rawlings ND, Polgár L, Barrett AJ. 1991. A new family of serine-type peptidases related to prolyl oligopeptidase. Biochem J 279:907-911.
    • (1991) Biochem J , vol.279 , pp. 907-911
    • Rawlings, N.D.1    Polgár, L.2    Barrett, A.J.3
  • 28
    • 0026026164 scopus 로고
    • CDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue
    • Rennex D, Hemmings BA, Hofsteenge J, Stone SR. 1991. cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue. Biochemistry 30:195-2203.
    • (1991) Biochemistry , vol.30 , pp. 195-2203
    • Rennex, D.1    Hemmings, B.A.2    Hofsteenge, J.3    Stone, S.R.4
  • 29
    • 0027315905 scopus 로고
    • Synthesis of mammalian prolyl endopeptidase in Escherichia coli and analysis of the recombinant protein
    • Sommer J. 1993. Synthesis of mammalian prolyl endopeptidase in Escherichia coli and analysis of the recombinant protein. Biochim Biophys Acta 1173:289-293.
    • (1993) Biochim Biophys Acta , vol.1173 , pp. 289-293
    • Sommer, J.1
  • 30
    • 0025890346 scopus 로고
    • Inactivation of prolyl endopeptidase by a peptidyl chloromethane. Kinetics of inactivation and identification of sites of modification
    • Stone SR, Rennex D, Wikstrom P, Shaw E, Hofsteenge J. 1991. Inactivation of prolyl endopeptidase by a peptidyl chloromethane. Kinetics of inactivation and identification of sites of modification. Biochem J 276:837-840.
    • (1991) Biochem J , vol.276 , pp. 837-840
    • Stone, S.R.1    Rennex, D.2    Wikstrom, P.3    Shaw, E.4    Hofsteenge, J.5
  • 31
    • 0027406861 scopus 로고
    • A comparison of the properties and enzymatic activities of three angiotensin processing enzyme: Angiotensin converting enzyme, prolyl endopeptidase and neutral endopeptidase
    • Welches WR, Brosnihan KB, Ferrario CM. 1993. A comparison of the properties and enzymatic activities of three angiotensin processing enzyme: Angiotensin converting enzyme, prolyl endopeptidase and neutral endopeptidase. Life Sci 52:1461-1480.
    • (1993) Life Sci , vol.52 , pp. 1461-1480
    • Welches, W.R.1    Brosnihan, K.B.2    Ferrario, C.M.3
  • 32
    • 0021084784 scopus 로고
    • Prolyl endopeptidase
    • Wilk S. 1983. Prolyl endopeptidase. Life Sci 33:2149-2157.
    • (1983) Life Sci , vol.33 , pp. 2149-2157
    • Wilk, S.1
  • 33
    • 0033577733 scopus 로고    scopus 로고
    • Loss of prolyl oligopeptidase confers resistance to lithium by elevation of inisitol(1,4,5)trisphosphate
    • Williams RSB, Eames M, Ryves WJ, Viggars J, Harwood AJ. 1999. Loss of prolyl oligopeptidase confers resistance to lithium by elevation of inisitol(1,4,5)trisphosphate. EMBO J 18:2734-2745.
    • (1999) EMBO J , vol.18 , pp. 2734-2745
    • Williams, R.S.B.1    Eames, M.2    Ryves, W.J.3    Viggars, J.4    Harwood, A.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.