Evolution of enzymatic activities in the enolase superfamily: crystal structure of (D)-glucarate dehydratase from Pseudomonas putida.
Gulick, A M
Evolution of enzymatic activities in the enolase superfamily: crystal structure of (D)-glucarate dehydratase from Pseudomonas putida. [electronic resource] - Biochemistry Oct 1998 - 14358-68 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.
0006-2960
10.1021/bi981123n doi
Amino Acid Sequence
Crystallization
Crystallography, X-Ray
Enzyme Activation
Evolution, Molecular
Hydro-Lyases--chemistry
Models, Molecular
Molecular Sequence Data
Peptide Fragments--chemistry
Phosphopyruvate Hydratase--chemistry
Protein Structure, Secondary
Protein Structure, Tertiary
Pseudomonas putida--enzymology
Racemases and Epimerases--chemistry
Sequence Alignment
Sequence Homology, Amino Acid
Structure-Activity Relationship
Evolution of enzymatic activities in the enolase superfamily: crystal structure of (D)-glucarate dehydratase from Pseudomonas putida. [electronic resource] - Biochemistry Oct 1998 - 14358-68 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.
0006-2960
10.1021/bi981123n doi
Amino Acid Sequence
Crystallization
Crystallography, X-Ray
Enzyme Activation
Evolution, Molecular
Hydro-Lyases--chemistry
Models, Molecular
Molecular Sequence Data
Peptide Fragments--chemistry
Phosphopyruvate Hydratase--chemistry
Protein Structure, Secondary
Protein Structure, Tertiary
Pseudomonas putida--enzymology
Racemases and Epimerases--chemistry
Sequence Alignment
Sequence Homology, Amino Acid
Structure-Activity Relationship