메뉴 건너뛰기




Volumn 59, Issue 2, 2002, Pages 349-362

The prolyl oligopeptidase family

Author keywords

propeller structure; Acylaminoacyl peptidase; Catalytic mechanism; Dipeptidyl peptidase; Oligopeptidase B; Oligopeptidases; Prolyl oligopeptidase; Serine peptidases

Indexed keywords

DIPEPTIDYL PEPTIDASE IV; PROLYL ENDOPEPTIDASE; SUBTILISIN; TRYPSIN;

EID: 0036178438     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-002-8427-5     Document Type: Review
Times cited : (284)

References (156)
  • 4
    • 0026669767 scopus 로고
    • Structural relationship between lipases and peptidases of the prolyl oligopeptidase family
    • (1992) FEBS Lett. , vol.311 , pp. 281-284
    • Polgár, L.1
  • 9
    • 0017085135 scopus 로고
    • Post-proline cleaving enzyme. Purification of this endopeptidase by affinity chromatography
    • (1976) J. Biol. Chem. , vol.251 , pp. 7593-7599
    • Koida, M.1    Waiter, R.2
  • 12
    • 0024291209 scopus 로고
    • Proline residues in the maturation and degradation of peptide-hormones and neuropeptides
    • (1988) FEBS Lett. , vol.234 , pp. 251-2566
    • Mentlein, R.1
  • 15
    • 0034003936 scopus 로고    scopus 로고
    • Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase family
    • (2000) Protein Sci. , vol.9 , pp. 353-360
    • Szeltner, Z.1    Renner, V.2    Polǵr, L.3
  • 34
    • 0020615453 scopus 로고
    • Inhibition of rabbit brain prolyl endopeptidase by N-benzyloxycarbonyl-prolyl-prolinal, a transition state aldehyde inhibitor
    • (1983) J. Neurochem. , vol.41 , pp. 69-75
    • Wilk, S.1    Orlowski, M.2
  • 44
    • 0027406861 scopus 로고
    • A comparison of the properties and enzymatic activities of three angiotensin processing enzymes: Angiotensin converting enzyme, prolyl endopeptidase and neutral endopeptidase
    • (1993) Life Sci. , vol.52 , pp. 1461-1480
    • Welches, W.R.1    Brosnihan, K.B.2    Ferrario, C.M.3
  • 62
    • 0025762537 scopus 로고
    • pH-Dependent mechanism in the catalysis of prolyl endopeptidase from pig muscle
    • (1991) Eur. J. Biochem. , vol.197 , pp. 441-447
    • Polgár, L.1
  • 64
    • 0028826743 scopus 로고
    • Effects of ionic strength on the catalysis and stability of prolyl oligopeptidase
    • (1995) Biochem. J. , vol.312 , pp. 267-271
    • Polgár, L.1
  • 65
    • 0027309007 scopus 로고
    • Prolyl oligopeptidase catalysis: Reactions with thiono substrates reveal substrate-induced conformational change to be the rate-limiting step
    • (1993) FEBS Lett. , vol.322 , pp. 227-230
    • Polgár, L.1    Kollát, E.2    Hollósi, M.3
  • 66
    • 0026550666 scopus 로고
    • Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting
    • (1992) Biochem J. , vol.283 , pp. 647-648
    • Polgár, L.1
  • 81
    • 0017252915 scopus 로고
    • Purificatioön of protease II from Escherichia coli by affinity chromatography and separation of two enzyme species from cells harvested at late log phase
    • (1976) Eur. J. Biochem. , vol.64 , pp. 199-104
    • Pacaud, M.1
  • 89
    • 0033598740 scopus 로고    scopus 로고
    • Oligopeptidase B: A new type of serine peptidase with a unique substrate-dependent temperature-sensitivity
    • (1999) Biochemistry , vol.38 , pp. 15548-15555
    • Polgár, L.1
  • 119
    • 0024516896 scopus 로고
    • Primary structure of rat liver dipeptidyl-peptidase IV deduced from its cDNA and identification of the NH2-terminal signal sequence as the membrane-anchoring domain
    • (1989) J. Biol. Chem. , vol.264 , pp. 3596-3601
    • Ogata, S.1    Misumi, Y.2    Ikehara, Y.3
  • 123
    • 0027236545 scopus 로고
    • Identification of serine 624, aspartic acid 702 and histidine 734 as the catalytic triad residues of mouse dipeptidyl-peptidase IV (CD26). A member of a novel family of nonclassical serine hydrolases
    • (1993) J. Biol. Chem. , vol.268 , pp. 17247-17252
    • David, F.1    Bernard, A.M.2    Pierres, M.3    Marguet, D.4
  • 138
    • 0027305358 scopus 로고
    • Separation of LPro-DL-boroPro into its component diastereomers and kinetic analysis of their inhibition of dipeptidyl peptidase IV. A new method for the analysis of slow, tight-binding inhibition
    • (1993) Biochemistry , vol.32 , pp. 8723-8731
    • Gutheil, W.G.1    Bachovchin, W.W.2
  • 143
  • 145
    • 0027265970 scopus 로고
    • Bovine lens acylpeptide hydrolase. Purification and characterization of a tetrameric enzyme resistant to urea denaturation and proteolytic inactivation
    • (1993) Eur. J. Biochem. , vol.216 , pp. 631-637
    • Sharma, K.K.1    Ortwerth, B.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.