Benzophenone boronic acid photoaffinity labeling of subtilisin CMMs to probe altered specificity.

[1]  W. A. Loughlin.  Biotransformations in organic synthesis , 2000 .

[2]  J. B. Jones,et al.  Toward Understanding and Tailoring the Specificity of Synthetically Useful Enzymes , 1999 .

[3]  J. Steghens,et al.  Identification of the creatine binding domain of creatine kinase by photoaffinity labeling. , 1998, Biochimica et biophysica acta.

[4]  Lewis E. Kay,et al.  Protein dynamics from NMR , 1998, Nature Structural Biology.

[5]  J. B. Jones,et al.  Site-directed mutagenesis combined with chemical modification as a strategy for altering the specificity of the S1 and S1' pockets of subtilisin Bacillus lentus. , 1998, Biochemistry.

[6]  G. Prestwich,et al.  Photoaffinity labeling of oxidosqualene cyclase and squalene cyclase by a benzophenone-containing inhibitor. , 1998, Biochemistry.

[7]  Chi‐Huey Wong,et al.  Biocatalysis and biotransformation Exploiting nature's magic , 1998 .

[8]  R. Schevitz,et al.  New trends in macromolecular X-ray crystallography. , 1997, Current opinion in chemical biology.

[9]  R. Cooke.  Protein NMR extends into new fields of structural biology. , 1997, Current opinion in chemical biology.

[10]  J. Stroh,et al.  Identification of a Firefly Luciferase Active Site Peptide Using a Benzophenone-based Photooxidation Reagent* , 1997, The Journal of Biological Chemistry.

[11]  J. B. Jones,et al.  Chemical Modification of Cysteine Mutants of Subtilisin Bacillus lentus Can Create Better Catalysts Than the Wild-Type Enzyme , 1997 .

[12]  G. Prestwich,et al.  Benzophenone Photoprobes for Phosphoinositides, Peptides and Drugs , 1997, Photochemistry and photobiology.

[13]  C. J. Murray,et al.  Active-site titration of serine proteases using a fluoride ion selective electrode and sulfonyl fluoride inhibitors. , 1996, Analytical biochemistry.

[14]  J. B. Jones,et al.  Probing the specificity of the S1 binding site of M222 mutants of subtilisin B. lentus with boronic acid inhibitors , 1996 .

[15]  J. B. Jones,et al.  Altering the specificity of subtilisin B. Lentus by combining site-directed mutagenesis and chemical modification , 1996 .

[16]  F. Richards,et al.  Mobile unnatural amino acid side chains in the core of staphylococcal nuclease , 1996, Protein science : a publication of the Protein Society.

[17]  J. B. Jones,et al.  Probing the Specificity of the Serine Proteases Subtilisin Carlsberg and α-Chymotrypsin with Enantiomeric 1-Acetamido Boronic Acids. An Unexpected Reversal of the Normal “l”-Stereoselectivity Preference , 1996 .

[18]  J. B. Jones,et al.  Probing the Abilities of Synthetically Useful Serine Proteases To Discriminate between the Configurations of Remote Stereocenters Using Chiral Aldehyde Inhibitors , 1996 .

[19]  Chi‐Huey Wong,et al.  Engineering Enzymes for Bioorganic Synthesis: Peptide Bond Formation , 1996 .

[20]  J. Kirsch,et al.  Examining the structural and chemical flexibility of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with unnatural amino acids. , 1995, Biochemistry.

[21]  M. Goeldner,et al.  Recent Trends in Photoaffinity Labeling , 1995 .

[22]  P. Sharp,et al.  Dynamic association of proteins with the pre-mRNA branch region. , 1994, Genes & development.

[23]  C. Paech,et al.  Peptide mapping of subtilisins as a practical tool for locating protein sequence errors during extensive protein engineering projects. , 1994, Analytical biochemistry.

[24]  George M. Whitesides,et al.  Enzymes in Synthetic Organic Chemistry , 1994 .

[25]  G. Prestwich,et al.  Benzophenone photophores in biochemistry. , 1994, Biochemistry.

[26]  R. London,et al.  Fluorine-19 NMR Studies of Fluorobenzeneboronic Acids. 2. Kinetic Characterization of the Interaction with Subtilisin Carlsberg and Model Ligands , 1994 .

[27]  J. B. Jones,et al.  Probing the specificity of the S1 binding site of subtilisin Carlsberg with boronic acids. , 1994, Bioorganic & medicinal chemistry.

[28]  J. Brunner,et al.  New photolabeling and crosslinking methods. , 1993, Annual review of biochemistry.

[29]  W. Bachovchin,et al.  Identification of serine and histidine adducts in complexes of trypsin and trypsinogen with peptide and nonpeptide boronic acid inhibitors by 1H NMR spectroscopy. , 1992, Biochemistry.

[30]  M. Sigman,et al.  Free energy and structure dependence of intramolecular triplet energy transfer in organic model compounds , 1991 .

[31]  P. Bonneau,et al.  Alteration of the specificity of subtilisin BPN' by site-directed mutagenesis in its S1 and S1' binding sites , 1991 .

[32]  K. Breddam,et al.  A highly active and oxidation-resistant subtilisin-like enzyme produced by a combination of site-directed mutagenesis and chemical modification. , 1990, European journal of biochemistry.

[33]  F. C. Hartman,et al.  Restoration of activity to catalytically deficient mutants of ribulosebisphosphate carboxylase/oxygenase by aminoethylation. , 1988, The Journal of biological chemistry.

[34]  K. Breddam,et al.  Chemical modifications of a cysteinyl residue introduced in the binding site of carboxypeptidase Y by site-directed mutagenesis , 1988, Carlsberg research communications.

[35]  S. Waley,et al.  A quick method for the determination of inhibition constants. , 1982, The Biochemical journal.

[36]  N. Mataga,et al.  Exciplex emissions of intra- and intermolecular benzophenone and N,N-dimethylaniline systems , 1981 .

[37]  E. G. Delmar,et al.  A sensitive new substrate for chymotrypsin. , 1979, Analytical biochemistry.

[38]  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.

[39]  Richard Wolfenden,et al.  Analog approaches to the structure of the transition state in enzyme reactions , 1972 .

[40]  G. Lienhard,et al.  2-phenylethaneboronic acid, a possible transition-state analog for chymotrypsin. , 1971, Biochemistry.

[41]  K. Courtney,et al.  A new and rapid colorimetric determination of acetylcholinesterase activity. , 1961, Biochemical pharmacology.