Penicillopepsin

Handbook of Proteolytic Enzymes, Second Edition: Volume 1: Aspartic and Metallo Peptidases

Volumn 1, Issue , 2004, Pages 99-104

  Hofmann, Theo ^a  

^a UNIVERSITY OF TORONTO   (Canada)

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[No Author keywords available]

Indexed keywords

EID: 57649219258     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-079611-3.50031-8     Document Type: Chapter

References (46)

1. C. Abad-Zapatero, T.J. Rydel and J. Erickson (1990) Revised 2.3Å structure of porcine pepsin: evidence for a flexible subdomain. Proteins Struct. Funct. Genet. 8 62-81.
2. B. Allen, M. Blum, A. Cunningham, G.-C. Tu and T. Hofmann (1990) A ligand-induced, temperature-dependent conformational change in penicillopepsin. J. Biol. Chem. 265 5060-5065.
3. V.K. Antonov, L.M. Ginodman, L.D. Rumsh, Y.K. Kapitannikov, T.N. Barshevskaya, L.P. Yavashev, A.G. Gurova and L.I. Volkova (1981) Studies on the mechanism of action of proteolytic enzymes using heavy oxygen exchange. Eur. J. Biochem. 117 195-200.
4. M. Balbaa, A. Cunningham and T. Hofmann (1993) Secondary substrate binding in aspartic proteinases: contributions of subsites S′ 2and S3to k cat. Arch. Biochem. Biophys. 306 297-303.
5. M. Balbaa, M. Blum and T. Hofmann (1994) Mechanism of pepsin-catalyzed aminotranspeptidation reactions. Int. J. Biochem. 26 35-42.
6. R.M. Berka, M. Ward, L.J. Wilson, K.J. Hayenga, K.H. Kodama, L.P. Carlomagno and S.A. Thompson (1990) Molecular cloning and deletion of the gene encoding aspergillopepsin A from Aspergillus awamori. Gene 86 153-162.
7. M. Blum, A. Cunningham, M. Bendiner and T. Hofmann (1985) Penicillopepsin, the aspartic proteinase from Penicillium janthinellum: substrate-binding effects and intermediates in transpeptidation reactions. Biochem. Soc. Trans. 13 1044-1047.
8. M. Blum, A. Cunningham, H. Pang and T. Hofmann (1991) Mechanism and pathway of penicillopepsin-catalyzed transpeptidation and evidence for noncovalent trapping of amino acid and peptide intermediates. J. Biol. Chem. 266 9501-9507.
9. E. Bracq, A. Levieux and D. Levieux (1997) Purification and immunochemical quantitation of Penicillium roqueforti aspartyl proteinase. J. Dairy Sci. 64 105-113.
10. Q.N. Cao, M. Stubbs, K.Q.P. Ngo, M. Ward, A. Cunningham, E.F. Pai, G.C. Tu and T. Hofmann (2000) Penicillopepsin-JT2, a recombinant enzyme from Penicillium janthinellum and the contribution of a hydrogen bond in subsite S3 to k cat. Protein Sci. 9 991-1001.
11. J. Chrzanowska, M. Kolaczkowska, M. Dryjansky, D. Stachowiak and A. Polanowski (1995) Aspartic proteinase from Penicillium camemberti: purification, properties, and substrate specificity. Enzyme Microb. Technol. 17 719-724.
12. J.B. Cooper, G. Khan, G. Taylor, I.J. Tickle and T.L. Blundell (1990) X-ray analysis of aspartic proteinases. II. Three-dimensional structure of the hexagonal form of porcine pepsin at 2.3Å resolution. J. Mol. Biol. 214 199-220.
13. A. Cunningham, M.I. Hofmann and T. Hofmann (1990) Rate-determining steps in penicillopepsin catalyzed reactions. FEBS Lett. 276 119-122.
14. S. Emi, D.V. Myers and G.A. Iacobucci (1976) Purification and properties of the thermostable acid protease of Penicillium duponti. Biochemistry 15 842-848.
15. M.E. Fraser, N.C. Strynadka, P.A. Bartlett, J.E. Hanson and M.N.G. James (1992) Crystallographic analysis of transition-state mimics bound to penicillopepsin: phosphorus-containing peptide analogues. Biochemistry 31 5201-5214.
16. J.S. Fruton (1970) The specificity and mechanism of pepsin action. Adv. Enzymol. Relat. Areas Mol. Biol. 33 401-443.
17. M. Fusek and V. Vetvicka (Eds) (1995) Aspartic Proteinases. Physiology and Pathology Boca Raton, FL: CRC Press 289-302.
18. T. Hofmann (1960) On the mechanism of activation of trypsinogen by penicillium kinase. Bull. Soc. Chim. Biol. 42 1279-1284.
19. T. Hofmann (1976) Penicillopepsin. Methods Enzymol. 45 434-452.
20. T. Hofmann and R. Shaw (1964) Proteolytic enzymes of Penicillium janthinellum. I. Purification and properties of a trypsinogen-activating enzyme (peptidase A). Biochim. Biophys. Acta 92 543-557.
21. T. Hofmann, R.S. Hodges and M.N.G. James (1984) Effect of pH on the activities of penicillopepsin and rhizopuspepsin, and a proposal for the productive substrate binding mode in penicillopepsin. Biochemistry 23 635-643.
22. T. Hofmann, B. Allen, M. Bendiner, M. Blum and A. Cunningham (1988) The effect of secondary substrate binding in penicillopepsin: the contributions of subsites S′2and S3to k cat. Biochemistry 27 1140-1147.
23. H. Horiuchi, K. Yanai, T. Okazaki, M. Takagi and K. Yano (1988) Isolation and sequencing of a genomic clone encoding aspartic proteinase of Rhizopus niveus. J. Bacteriol. 170 272-278.
24. I.N. Hsu, L.T.J. Delbaere, M.N.G. James and T. Hofmann (1977) Penicillopepsin from Penicillium janthinellum: crystal structure at 2.8Å and sequence homology with porcine pepsin. Nature (London) 266 140-145.
25. M.N.G. James and A.R. Sielecki (1983) Structure and refinement of penicillopepsin at 1.8Å resolution. J. Mol. Biol. 163 299-361.
26. M.N.G. James and A.R. Sielecki (1985) Stereochemical analysis of peptide bond hydrolysis catalyzed by the aspartic proteinase penicillopepsin. Biochemistry 24 3701-3713.
27. M.N.G. James, A.R. Sielecki, F. Salituro, D.H. Rich and T. Hofmann (1982) Conformational flexibility in the active sites of aspartyl proteinases revealed by a pepstatin fragment binding to penicillopepsin. Proc. Natl. Acad. Sci. USA 79 6137-6141.
28. M.N.G. James, A.R. Sielecki and T. Hofmann (1985) X-ray diffraction studies on penicillopepsin and its complexes: the hydrolytic mechanism. V. Kostka (Ed.) Aspartic Proteinases and Their Inhibitors Berlin: Walter de Gruyter 163-177.
29. M.N.G. James, A.R. Sielecki, K. Hayakawa and M.H. Gelb (1992) Crystallographic analysis of transition-state mimics bound to penicillopepsin: difluorostatine- and difluorostatone-containing peptides. Biochemistry 31 3872-3886.
30. A.R. Khan, J.C. Parrish, M.E. Fraser, W.W. Smith, P.A. Bartlett and M.N.G. James (1998) Lowering the entropic barrier for binding conformationally flexible inhibitors to enzymes. Biochemistry 37 16839-16845.
31. M. Kunitz (1938) Formation of trypsin from trypsinogen by an enzyme produced by a mold of the genus Penicillium. J. Gen. Physiol. 21 601-620.
32. W.T. Lowther, P. Majer and B.M. Dunn (1995) Engineering the substrate specificity of rhizopuspepsin: the role of Asp 77 of fungal aspartic proteinases in facilitating the cleavage of oligopeptide substrates with lysine in P1. Protein Sci. 4 689-702.
33. G. Mains, M. Takahashi, J. Sodek and T. Hofmann (1971) The specificity of penicillopepsin. Can. J. Biochem. 49 1134-1149.
34. K. Nakanishi (1959) Trypsinogen-kinase in Aspergillus oryzae. III. Purification of trypsinogen kinase and its relation to acid-protease. J. Biochem. (Tokyo) 46 1263-1269.
35. J. Otlewski, A. Polanowski, J. Leluk and T. Wilusz (1984) Trypsin inhibitors in summer squash (Cucurbita pepo) seeds. Isolation, purification and partial characterization of three inhibitors. Acta Biochim. Polon. 31 267-278.
36. Rawlings, N.D. & Barrett, A.J. (2002) MEROPS — The Peptidase Database (merops.sanger.co.uk/merops/merops.htm).
37. V. Razanamparany, P. Jara, R. Legoux, P. Delmas, F. Msayeh, M. Kaghad and G. Loison (1992) Cloning and mutation of the gene encoding endothiapepsin from Cryphonectria parasitica. Curr. Genet. 21 455-461.
38. A. Sali, B. Veerapandian, J.B. Cooper, D.S. Moss, T. Hofmann and T.L. Blundell (1992) Domain flexibility in aspartic proteinases. Proteins Struct. Funct. Genet. 12 158-170.
39. P. Sepulveda, J. Marciniszyn, D. Liu and J. Tang (1975) Primary structure of porcine pepsin. III. Amino acid sequence of a cyanogen bromide fragment, CB2A, and the complete structure of porcine pepsin. J. Biol. Chem. 250 5082-5088.
40. R. Shaw and T. Hofmann (1964) Proteolytic enzymes of Penicillium janthinellum. I. Purification and properties of a trypsinogen-activating enzyme (peptidase A). Biochim. Biophys. Acta 92 543-557.
41. A.R. Sielecki, A.A. Fedorov, A. Boodhoo, N.S. Andreeva and M.N.G. James (1990) Molecular and crystal structure of mon-oclinic porcine pepsin refined at 1.8 Å resolution. J. Mol. Biol. 214 143-170.
42. J. Sodek and T. Hofmann (1970) Amino acid sequence around the active site aspartic acid in penicillopepsin. Can. J. Biochem. 48 1014-1016.
43. A. Thangamani and T. Hofmann (1966) The role of a protease in the sporulation of Penicillium janthinellum. Can. J. Biochem. 44 579-584.
44. N. Tonouchi, H. Shoun, T. Uozumi and T. Beppu (1986) Cloning and sequencing of a gene for mucor rennin, an aspartic proteinase from Mucor pusillus. Nucleic Acids Res. 14 7551-7568.
45. T.T. Wang and T. Hofmann (1976) Acyl and amino intermediates in reactions catalysed by pig pepsin. Biochem. J. 153 691-699.
46. C. Zevaco, J. Hermier and J.-C. Gripon (1973) Le systéme protéolytique de Penicillium roqueforti. II. Purification et propriétés de la protéase acide [The proteolytic system of Penicillium roqueforti. II. Purification and properties of the acid protease]. Biochimie 55 1353-1360.