Asp333, Asp495, and His523 form the catalytic triad of rat soluble epoxide hydrolase.
Arand, M
Asp333, Asp495, and His523 form the catalytic triad of rat soluble epoxide hydrolase. [electronic resource] - The Journal of biological chemistry Feb 1996 - 4223-9 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
0021-9258
10.1074/jbc.271.8.4223 doi
Amino Acid Sequence
Animals
Aspartic Acid
Binding Sites
Catalysis
Cloning, Molecular
DNA Primers
Epoxide Hydrolases--biosynthesis
Escherichia coli
Histidine
Humans
Kinetics
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Point Mutation
Polymerase Chain Reaction
Protein Structure, Secondary
Rats
Recombinant Proteins--biosynthesis
Restriction Mapping
Sequence Homology, Amino Acid
Asp333, Asp495, and His523 form the catalytic triad of rat soluble epoxide hydrolase. [electronic resource] - The Journal of biological chemistry Feb 1996 - 4223-9 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
0021-9258
10.1074/jbc.271.8.4223 doi
Amino Acid Sequence
Animals
Aspartic Acid
Binding Sites
Catalysis
Cloning, Molecular
DNA Primers
Epoxide Hydrolases--biosynthesis
Escherichia coli
Histidine
Humans
Kinetics
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Point Mutation
Polymerase Chain Reaction
Protein Structure, Secondary
Rats
Recombinant Proteins--biosynthesis
Restriction Mapping
Sequence Homology, Amino Acid