Handbook of Proteolytic Enzymes. Aspartic and Metallo by Alan J. Barrett, J. Fred Woessner and Neil D. Rawlings

By Alan J. Barrett, J. Fred Woessner and Neil D. Rawlings (Eds.)

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1976) Conversion of pepsinogen into pepsin is not a one-step process. Biochem. J. 153, 141-144. W. R. (1989) Nucleotide sequence comparison of five human pepsinogen A (PGA) genes: evolution of the PGA multigene family. Genomics 4, 232-239. , Parisoli, A. & Mazzini, A. (1997) Alkaline denaturation and partial refolding of pepsin investigated with DAPI as an extrinsic probe. Biophys. Chem. 67, 75-83. Foltmann, B. (1988) Activation of human pepsinogens. FEBS Lett. 241, 69-72. S. (1971) Pepsin. ), New York: Academic Press, pp.

5 A proposed configuration of the two aspartic acid residues and the bound water in the HIV proteinase structure as deduced from ab initio molecular dynamics simulations (Piana & Carloni, 2000). 1). , 2001) of a transition state analog inhibitor, H261, complexed to endothiapepsin has determined with reasonable certainty the protonation states of the active-site groups in this reduced peptide complex. e. negatively charged, and Asp219 (215) is protonated. 3(B) and (C). It would have been more convincing had the neutron study been undertaken with an inhibitor that more closely represented the transition state, such as the hydrated difluorostatone.

Funct. Genet. 13, 1-25. F. (1981) The cells of the gastric mucosa. Int. Rev. Cytol. 70, 217-289. M. (1938) Isolation, crystallization and properties of swine pepsinogen. J. Gen. Physiol. 21, 501-540. , Desreux, V. H. (1940) Electrophoresis of pepsin. J. Gen. Physiol. 23, 439-447. , Zundel, G. & Brzezinski, B. (1997) Catalytic mechanism of the aspartate proteinase pepsin A: an FTIR study. BiospectroscopyX 291-297. G. R. 8 Ä resolution. Nature 319, 33-38. Kageyama, T. (1998) Molecular cloning, expression and characterization of an Ascaris inhibitor for pepsin and cathepsin E.

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