Evolutionary Divergence of Substrate Specificity within the Chymotrypsin-like Serine Protease Fold*
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C. Craik | J. Perona | J J Perona | C S Craik
[1] D. Agard,et al. Serine protease mechanism: structure of an inhibitory complex of alpha-lytic protease and a tightly bound peptide boronic acid. , 1987, Biochemistry.
[2] R J Fletterick,et al. Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix. , 1997, Biochemistry.
[3] R. Fletterick,et al. Structural basis for the broad substrate specificity of fiddler crab collagenolytic serine protease 1. , 1997, Biochemistry.
[4] W. Rutter,et al. Converting trypsin to chymotrypsin: the role of surface loops. , 1992, Science.
[5] R. Kurumbail,et al. Three-dimensional structure of human cytomegalovirus protease , 1996, Nature.
[6] W. Rutter,et al. Redesigning trypsin: alteration of substrate specificity. , 1985, Science.
[7] David A. Agard,et al. Structural plasticity broadens the specificity of an engineered protease , 1989, Nature.
[8] C. Craik,et al. Substrate specificity of trypsin investigated by using a genetic selection. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[9] A. Berger,et al. On the size of the active site in proteases. I. Papain. , 1967, Biochemical and biophysical research communications.
[10] R J Fletterick,et al. Relocating a negative charge in the binding pocket of trypsin. , 1994, Journal of molecular biology.
[11] Patricia C. Babbitt,et al. Understanding Enzyme Superfamilies , 1997, The Journal of Biological Chemistry.
[12] T. Steitz,et al. Crystallographic and NMR studies of the serine proteases. , 1982, Annual review of biophysics and bioengineering.
[13] W. Rutter,et al. Exogenous acetate reconstitutes the enzymatic activity of trypsin Asp189Ser. , 1994, Biochemistry.
[14] S Farr-Jones,et al. Converting trypsin to chymotrypsin: ground-state binding does not determine substrate specificity. , 1994, Biochemistry.
[15] H. Muirhead,et al. A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework. , 1988, Science.
[16] E. Goldsmith,et al. Amino acid residues that affect interaction of tissue-type plasminogen activator with plasminogen activator inhibitor 1. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[17] P. Bonneau,et al. A new serine-protease fold revealed by the crystal structure of human cytomegalovirus protease , 1996, Nature.
[18] C. Ponting,et al. The crystal structure of the catalytic domain of human urokinase-type plasminogen activator. , 1995, Structure.
[19] Robert Huber,et al. The refined 1.9 A crystal structure of human alpha‐thrombin: interaction with D‐Phe‐Pro‐Arg chloromethylketone and significance of the Tyr‐Pro‐Pro‐Trp insertion segment. , 1989 .
[20] David A. Matthews,et al. Structure of the Human Cytomegalovirus Protease Catalytic Domain Reveals a Novel Serine Protease Fold and Catalytic Triad , 1996, Cell.
[21] C. Turck,et al. The substrate specificity of Uca pugilator collagenolytic serine protease 1 correlates with the bovine type I collagen cleavage sites. , 1994, The Journal of biological chemistry.
[22] C. Craik,et al. Structural basis of substrate specificity in the serine proteases , 1995, Protein science : a publication of the Protein Society.
[23] S. Remington,et al. Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A new class of serine proteinase. , 1991, The Journal of biological chemistry.
[24] W. Rutter,et al. Selective alteration of substrate specificity by replacement of aspartic acid-189 with lysine in the binding pocket of trypsin. , 1987, Biochemistry.
[25] A. Rehemtulla,et al. Cloning and functional expression of a cDNA encoding the catalytic subunit of bovine enterokinase. , 1993, The Journal of biological chemistry.
[26] J. Culp,et al. Unique fold and active site in cytomegalovirus protease , 1996, Nature.
[27] W. Rutter,et al. Converting trypsin to chymotrypsin: residue 172 is a substrate specificity determinant. , 1994, Biochemistry.
[28] J. Knowles,et al. Stepwise improvements in catalytic effectiveness: independence and interdependence in combinations of point mutations of a sluggish triosephosphate isomerase. , 1991, Biochemistry.
[29] R J Fletterick,et al. Engineered metal regulation of trypsin specificity. , 1995, Biochemistry.
[30] A. Dean,et al. A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[31] D. Agard,et al. Functional linkage between the active site of alpha-lytic protease and distant regions of structure: scanning alanine mutagenesis of a surface loop affects activity and substrate specificity. , 1995, Journal of molecular biology.
[32] D. Agard,et al. Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. , 1995, Journal of molecular biology.
[33] W. Rutter,et al. Structural origins of substrate discrimination in trypsin and chymotrypsin. , 1995, Biochemistry.
[34] L. DeLucas,et al. Structure of human factor D. A complement system protein at 2.0 A resolution. , 1994, Journal of molecular biology.