Structures of product and inhibitor complexes of Streptomyces griseus protease A at 1.8 A resolution. A model for serine protease catalysis.

[1]  L. Delbaere,et al.  Crystal structure studies and inhibition kinetics of tripeptide chloromethyl ketone inhibitors with Streptomyces griseus protease B. , 1980, Journal of molecular biology.

[2]  L. Delbaere,et al.  Protein structure refinement: Streptomyces griseus serine protease A at 1.8 A resolution. , 1979, Journal of molecular biology.

[3]  D. Phillips,et al.  Crystallographic studies of the dynamic properties of lysozyme , 1979, Nature.

[4]  梅山 秀明,et al.  A Molecular Orbital Study on the Complex between Aspartic Acid and Histidine in the Charge Relay Structure , 1979 .

[5]  L. Delbaere,et al.  Molecular structure of the α-lytic protease from Myxobacter 495 at 2·8 Å resolution☆ , 1979 .

[6]  L. Delbaere,et al.  The 2.8 A resolution structure of Streptomyces griseus protease B and its homology with alpha-chymotrypsin and Streptomyces griseus protease A. , 1979, Canadian Journal of Biochemistry.

[7]  John D. Roberts,et al.  Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of .alpha.-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteases , 1978 .

[8]  J. Markley,et al.  Zymogen activation in serine proteinases. Proton magnetic resonance pH titration studies of the two histidines of bovine chymotrypsinogen A and chymotrypsin Aalpha. , 1978, Biochemistry.

[9]  M. Perutz.  Electrostatic effects in proteins. , 1978, Science.

[10]  L. Delbaere,et al.  Molecular structure of crystalline Streptomyces griseus protease A at 2.8 A resolution. I. Crystallization, data collection and structural analysis. , 1978, Journal of molecular biology.

[11]  L. Delbaere,et al.  Molecular structure of crystalline Streptomyces griseus protease A at 2.8 A resolution. II. Molecular conformation, comparison with alpha-chymotrypsin and active-site geometry. , 1978, Journal of molecular biology.

[12]  L. Sieker,et al.  Water structure in a protein crystal: rubredoxin at 1.2 A resolution. , 1978, Journal of molecular biology.

[13]  H. Berendsen,et al.  The α-helix dipole and the properties of proteins , 1978, Nature.

[14]  L. Delbaere,et al.  Amino acid sequence alignment of bacterial and mammalian pancreatic serine proteases based on topological equivalences. , 1978, Canadian journal of biochemistry.

[15]  Robert M. Stroud,et al.  The accuracy of refined protein structures: comparison of two independently refined models of bovine trypsin , 1978 .

[16]  R. Huber,et al.  Structural basis of the activation and action of trypsin , 1978 .

[17]  C. Bauer.  Active centers of Streptomyces griseus protease 1, Streptomyces griseus protease 3, and alpha-chymotrypsin: enzyme-substrate interactions. , 1978, Biochemistry.

[18]  S. Yomosa,et al.  Molecular Orbital Studies on the Enzymatic Reaction Mechanism of Serine Proteases. II. Nucleophilic Attack of the O γ Atom of Ser-195 during the Acylation of α-Chymotrypsin , 1978 .

[19]  D. Matthews,et al.  Re-examination of the charge relay system in subtilisin comparison with other serine proteases. , 1977, The Journal of biological chemistry.

[20]  J. Fastrez,et al.  Mechanism of chymotrypsin: acid/base catalysis and transition-state solvation by the active site. , 1977, European journal of biochemistry.

[21]  I. Liener,et al.  Interaction of the Kunitz soybean trypsin inhibitor with bovine trypsin. Evidence for an an acy-enzyme intermediate during complexation. , 1977, Biochemistry.

[22]  S. Yomosa,et al.  Molecular Orbital studies on the Enzymatic Reaction Mechanism of Serine Proteases. I. Charge Relay System in Substrate Free State , 1977 .

[23]  J. Cohen,et al.  Characterization of the acetyl-chymotrypsin intermediate by 13C nuclear magnetic resonance spectroscopy. , 1977, Journal of the American Chemical Society.

[24]  J. Finney.  The organization and function of water in protein crystals. , 1977, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[25]  R. Thompson.  Peptide aldehydes: potent inhibitors of serine and cysteine proteases. , 1977, Methods in enzymology.

[26]  A. Fink,et al.  Reactivity and cryoenzymology of enzymes in the crystalline state. , 1977, Annual review of biophysics and bioengineering.

[27]  J. Kraut.  Serine proteases: structure and mechanism of catalysis. , 1977, Annual review of biochemistry.

[28]  G. Petsko,et al.  Crystal structure of elastase–substrate complex at −55 °C , 1976, Nature.

[29]  J. Konnert,et al.  A restrained-parameter structure-factor least-squares refinement procedure for large asymmetric units , 1976 .

[30]  David M. Blow,et al.  Structure and mechanism of chymotrypsin , 1976 .

[31]  E. Blout,et al.  The active centers of Streptomyces griseus protease 3 and alpha-chymotrypsin: enzyme-substrate interactions remote from the scissile bond. , 1976, Biochemistry.

[32]  E. Blout,et al.  The active centers of Streptomyces griseus protease 3, alpha-chymotrypsin, and elastase: enzyme-substrate interactions close to the scissile bond. , 1976, Biochemistry.

[33]  J. Kraut,et al.  Polypeptide halomethyl ketones bind to serine proteases as analogs of the tetrahedral intermediate. X-ray crystallographic comparison of lysine- and phenylalanine-polypeptide chloromethyl ketone-inhibited subtilisin. , 1976, The Journal of biological chemistry.

[34]  W. E. Thiessen,et al.  Tertiary structural differences between microbial serine proteases and pancreatic serine enzymes , 1975, Nature.

[35]  P. G. Lenhert,et al.  An adaptable disk-oriented automatic diffractometer control program , 1975 .

[36]  D. Matthews,et al.  X-ray crystallographic study of boronic acid adducts with subtilisin BPN' (Novo). A model for the catalytic transition state. , 1975, The Journal of biological chemistry.

[37]  R. Thompson.  Binding of peptides to elastase: implications for the mechanism of substrate hydrolysis. , 1974, Biochemistry.

[38]  L. Smillie,et al.  Amino acid sequence of Streptomyces griseus protease B, A MAJOR COMPONENT OF Pronase. , 1974, Biochemical and biophysical research communications.

[39]  J Deisenhofer,et al.  Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 A resolution. , 1974, Journal of molecular biology.

[40]  L. Smillie,et al.  The amino acid sequence and predicted structure of Streptomyces griseus protease A , 1974, FEBS letters.

[41]  R M Sweet,et al.  Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-A resolution. , 1974, Biochemistry.

[42]  A. Gertler.  Inhibition of Streptomyces griseus protease B by peptide chloromethyl ketones: Partial mapping of the binding site and identification of the reactive residue , 1974, FEBS letters.

[43]  G. Pettersson,et al.  Effect of pH on the catalytic activity of Streptomyces griseus protease 3. , 1974, European journal of biochemistry.

[44]  G A Rogers,et al.  Synthesis and evaluation of a model for the so-called "charge-relay" system of the serine esterases. , 1974, Journal of the American Chemical Society.

[45]  R. Dickerson,et al.  The structure of bovine trypsin : Electron density maps of the inhibited enzyme at 5 Å and at 2·7 Å resolution☆ , 1974 .

[46]  G. Pettersson,et al.  Studies on the catalytic mechanism of a serine protease from Streptomyces griseus. , 1974, European journal of biochemistry.

[47]  I. Kuntz,et al.  Hydration of proteins and polypeptides. , 1974, Advances in protein chemistry.

[48]  M. Hunkapiller,et al.  Carbon nuclear magnetic resonance studies of the histidine residue in alpha-lytic protease. Implications for the catalytic mechanism of serine proteases. , 1973, Biochemistry.

[49]  R. Huber,et al.  Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region. , 1973, Journal of molecular biology.

[50]  Jack D. Dunitz,et al.  Geometrical reaction coordinates. II. Nucleophilic addition to a carbonyl group , 1973 .

[51]  A. Fersht,et al.  Demonstration of the acyl-enzyme mechanism for the hydrolysis of peptides and anilides by chymotrypsin. , 1973, Biochemistry.

[52]  W. M. Awad,et al.  The proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). IV. Structure-function studies of the two smallest serine endopeptidases; stabilization by glycerol during reaction with acetic anhydride. , 1973, The Journal of biological chemistry.

[53]  R. Thompson.  Use of peptide aldehydes to generate transition-state analogs of elastase. , 1973, Biochemistry.

[54]  C. Bauer,et al.  Studies of the heterogeneity of Streptomyces griseus protease. Isolation and characterization of an alkaline serine protease from commercial pronase-P derived from Streptomyces griseus K1. , 1973, Acta chemica Scandinavica.

[55]  J. Kraut,et al.  Subtilisin; a stereochemical mechanism involving transition-state stabilization. , 1972, Biochemistry.

[56]  K. B. Birnbaum.  Structure and absolute configuration of the alkaloid clivorine , 1972 .

[57]  D. M. Blow,et al.  Structure of crystalline -chymotrypsin. V. The atomic structure of tosyl- -chymotrypsin at 2 A resolution. , 1972, Journal of molecular biology.

[58]  J. Kraut,et al.  An x-ray crystallographic study of the binding of peptide chloromethyl ketone inhibitors to subtilisin BPN'. , 1972, Biochemistry.

[59]  D. Segal.  A kinetic investigation of the crystallographically deduced binding subsites of bovine chymotrypsin A . , 1972, Biochemistry.

[60]  R. Martin.  O-protonation of amides in dilute acids , 1972 .

[61]  L. Smillie,et al.  An improved fractionation system for pronase on CM-sephadex. , 1971, Canadian journal of biochemistry.

[62]  G. Cohen,et al.  Substrate binding site in bovine chymotrypsin A-gamma. A crystallographic study using peptide chloromethyl ketones as site-specific inhibitors. , 1971, Biochemistry.

[63]  A. Gertler,et al.  The elastase-like enzymes from Streptomyces griseus (pronase). Isolation and partial characterization. , 1971, European journal of biochemistry.

[64]  D. W. Johnson,et al.  Measurement of Depolarization Ratios in the Raman Spectra of Powdered Crystalline Solids , 1971 .

[65]  S. Bernhard,et al.  On the relationship between the conformation and the catalyzed reactivity of acyl-chymotrypsin. , 1971, Journal of molecular biology.

[66]  R. Henderson.  Structure of crystalline alpha-chymotrypsin. IV. The structure of indoleacryloyl-alpha-chyotrypsin and its relevance to the hydrolytic mechanism of the enzyme. , 1970, Journal of molecular biology.

[67]  T. Steitz,et al.  X-ray diffraction studies of enzymes. , 1970, Annual review of biochemistry.

[68]  Y. Narahashi,et al.  Complete separation of three alkaline proteinases a, b, and c from pronase and some characteristics of alkaline proteinase b. , 1969, Journal of biochemistry.

[69]  D. Blow,et al.  Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin , 1969, Nature.

[70]  F M Richards,et al.  The matching of physical models to three-dimensional electron-density maps: a simple optical device. , 1968, Journal of molecular biology.

[71]  F. S. Mathews,et al.  A semi-empirical method of absorption correction , 1968 .

[72]  F. Ahmed,et al.  The crystal structure of cryptopine, C21H23O5N , 1968 .

[73]  S. Hall.  The crystal structure of protopine, C20H19O5N , 1968 .

[74]  S. Wählby.  Studies on Streptomyces griseus protease. I. Separation of DFP-reacting enzymes and purification of one of the enzymes. , 1968, Biochimica et biophysica acta.

[75]  S. Bernhard,et al.  Optical properties and the chemical nature of acyl-chymotrypsin linkages. , 1967, Journal of the American Chemical Society.

[76]  A. Berger,et al.  On the size of the active site in proteases. I. Papain. , 1967, Biochemical and biophysical research communications.

[77]  B. Hartley,et al.  Corrections to the amino acid sequence of bovine chymotrypsinogen A. , 1966, The Biochemical journal.

[78]  Berhard Sa,et al.  ACYL INTERMEDIATES IN THE ALPHA-CHYMOTRYPSIN-CATALYZED HYDROLYSIS OF INDOLEACRYLOYLIMIDAZOLE. , 1965 .

[79]  M. L. Bender.  The Mechanism of α-Chymotrypsin-catalyzed Hydrolyses1-3 , 1962 .

[80]  M. L. Bender,et al.  DIRECT SPECTROPHOTOMETRIC EVIDENCE FOR AN ACYL-ENZYME INTERMEDIATE IN THE CHYMOTRYPSIN-CATALYZED HYDROLYSIS OF O-NITROPHENYL CINNAMATE1 , 1959 .

[81]  B. Hartley,et al.  The reaction of p-nitrophenyl esters with chymotrypsin and insulin. , 1954, The Biochemical journal.