PPIase catalysis by human FK506-binding protein proceeds through a conformational twist mechanism.
Park, S T
PPIase catalysis by human FK506-binding protein proceeds through a conformational twist mechanism. [electronic resource] - The Journal of biological chemistry Feb 1992 - 3316-24 p. digital
Publication Type: Comparative Study; Journal Article
0021-9258
Amino Acid Isomerases--metabolism
Amino Acid Sequence
Animals
Base Sequence
Carrier Proteins--genetics
Cattle
Humans
Hydrogen-Ion Concentration
Kinetics
Molecular Sequence Data
Mutagenesis, Site-Directed
Neurospora crassa--metabolism
Oligodeoxyribonucleotides
Oligopeptides--chemical synthesis
Peptidylprolyl Isomerase
Protein Conformation
Recombinant Proteins--metabolism
Saccharomyces cerevisiae--metabolism
Sequence Homology, Nucleic Acid
Spectrometry, Fluorescence
Substrate Specificity
Tacrolimus--metabolism
Tacrolimus Binding Proteins
PPIase catalysis by human FK506-binding protein proceeds through a conformational twist mechanism. [electronic resource] - The Journal of biological chemistry Feb 1992 - 3316-24 p. digital
Publication Type: Comparative Study; Journal Article
0021-9258
Amino Acid Isomerases--metabolism
Amino Acid Sequence
Animals
Base Sequence
Carrier Proteins--genetics
Cattle
Humans
Hydrogen-Ion Concentration
Kinetics
Molecular Sequence Data
Mutagenesis, Site-Directed
Neurospora crassa--metabolism
Oligodeoxyribonucleotides
Oligopeptides--chemical synthesis
Peptidylprolyl Isomerase
Protein Conformation
Recombinant Proteins--metabolism
Saccharomyces cerevisiae--metabolism
Sequence Homology, Nucleic Acid
Spectrometry, Fluorescence
Substrate Specificity
Tacrolimus--metabolism
Tacrolimus Binding Proteins