Relationship of the three dimensional structure of carboxypeptidase A to catalysis

Abstract A brief discussion is presented of activity, conformational changes, possible mechanisms, intermediates, and pH effects in the peptidase activity of the hydrolytic enzyme, carboxypeptidase A.

[1]  A. Berger,et al.  On the size of the active site in proteases. II. Carboxypeptidase-A. , 1967, Biochemical and biophysical research communications.

[2]  H. Neurath,et al.  Modification of carboxyl groups in bovine carboxypeptidase A. II. Chemical identification of a functional glutamic acid residue and other reactive groups. , 1971, Biochemistry.

[3]  M. A. Stahmann,et al.  The specificity of carboxypeptidase. , 1940, The Journal of biological chemistry.

[4]  G. Reeke,et al.  The structure of carboxypeptidase A. IX. The x-ray diffraction results in the light of the chemical sequence. , 1969, Proceedings of the National Academy of Sciences of the United States of America.

[5]  E. L. Smith.  Action of carboxypeptidase on peptide derivatives of L-tryptophan. , 1948, The Journal of biological chemistry.

[6]  E. Kaiser,et al.  On the action of carboxypeptidase A on ester substrates in alkaline solution. , 1972, Biochemical and biophysical research communications.

[7]  Joseph E. Coleman,et al.  The Catalytic Mechanism of Carbonic Anhydrase , 1973 .

[8]  P. Pétra.  Modification of carboxyl groups in bovine carboxypeptidase A. I. Inactivation of the enzyme by N-ethyl-5-phenylisoxazolium-3'-sulfonate (Woodward's reagent K). , 1971, Biochemistry.

[9]  G. Reeke,et al.  The structure of carboxypeptidase a, vi. Some results at 2.0-a resolution, and the complex with glycyl-tyrosine at 2.8-a resolution. , 1967, Proceedings of the National Academy of Sciences of the United States of America.

[10]  H. Neurath,et al.  Affinity labeling of bovine carboxypeptidase A Leu by N-bromoacetyl-N-methyl-L-phenylalanine. II. Sites of modification. , 1971, Biochemistry.

[11]  F. Quiocho,et al.  Similarities between the conformation of arsanilazotyrosine 248 of carboxypeptidase A in the crystalline state and in solution. , 1972, Proceedings of the National Academy of Sciences of the United States of America.

[12]  F A Quiocho,et al.  Carboxypeptidase A: a protein and an enzyme. , 1971, Advances in protein chemistry.

[13]  D. Phillips,et al.  On the conformation of the hen egg-white lysozyme molecule , 1967, Proceedings of the Royal Society of London. Series B. Biological Sciences.

[14]  E. Kaiser,et al.  Carboxypeptidase A. Mechanistic analysis , 1972 .

[15]  W. Lipscomb.  Enzymatic activities of carobxypeptidase A's in solution and in crystals. , 1973, Proceedings of the National Academy of Sciences of the United States of America.

[16]  Kaiser Et,et al.  pH dependence of the hydrolysis of O-acetyl-L-mandelate catalyzed by carboxypeptidase A. A critical examination. , 1966 .

[17]  F. Quiocho,et al.  X-ray diffraction and nuclear magnetic resonance dispersion studies on derivatives of carboxypeptidase A. , 1972, Cold Spring Harbor symposia on quantitative biology.

[18]  H. Neurath,et al.  Affinity labeling of bovine carboxypeptidase A Leu by N-bromoacetyl-N-methyl-L-phenylalanine. I. Kinetics of inactivation. , 1971, Biochemistry.

[19]  D. Koshland.  Application of a Theory of Enzyme Specificity to Protein Synthesis. , 1958, Proceedings of the National Academy of Sciences of the United States of America.

[20]  W. Lipscomb.  Centenary Lecture. Three-dimensional structures and chemical mechanisms of enzymes , 1972 .

[21]  B. Matthews.  Solvent content of protein crystals. , 1968, Journal of molecular biology.

[22]  E. Kaiser,et al.  Effect of D2O on the carboxypeptidase-catalyzed hydrolysis of O-(trans-cinnamoyl)-L-beta-phenyllactate and N-(N-benzoylglycyl)-L-phenylalanine. , 1969, Proceedings of the National Academy of Sciences of the United States of America.

[23]  D. Livingston,et al.  Chemical modification of carboxypeptidase A crystals. Azo coupling with tyrosine-248. , 1972, Biochemistry.

[24]  J. Riordan,et al.  Carboxypeptidase A: approaches to the chemical nature of the active center and the mechanisms of action. , 1963, Proceedings of the National Academy of Sciences of the United States of America.

[25]  Dahlquist Fw,et al.  A nuclear magnetic resonance study of enzyme-inhibitor association. The use of pH and temperature effects to probe the binding environments. , 1968 .

[26]  B. Vallee,et al.  Conformations of Arsanilazotyrosine-248 Carboxypeptidase Aα,β,γ. Comparison of Crystals and Solution , 1973 .

[27]  M. Laskowski,et al.  Enzymatic replacement of the arginyl by a lysyl residue in the reactive site of soybean trypsin inhibitor. , 1969, Biochemistry.

[28]  M. Mitz,et al.  The Mode of Action of Pancreatic Carboxypeptidase. II. The Affinity of Carboxypeptidase for Substrates and Inhibitors1 , 1957 .