F
Frank M. Raushel
Researcher at Texas A&M University
Publications - 358
Citations - 15104
Frank M. Raushel is an academic researcher from Texas A&M University. The author has contributed to research in topics: Active site & Carbamoyl phosphate synthetase. The author has an hindex of 60, co-authored 351 publications receiving 14208 citations. Previous affiliations of Frank M. Raushel include Wayne State University & National Institutes of Health.
Papers
More filters
Journal ArticleDOI
Purification and properties of the phosphotriesterase from Pseudomonas diminuta.
TL;DR: The phosphotriesterase produced from the opd cistron of Pseudomonas diminuta was purified 1500-fold to homogeneity using a combination of gel filtration, ion exchange, hydrophobic, and dye matrix chromatographic steps, making it the first organophosphate triesterase or organoph phosphofluoridate hydrolyzing enzyme to be purified to homogeneous.
Journal ArticleDOI
Structural and catalytic diversity within the amidohydrolase superfamily.
TL;DR: The amidohydrolase superfamily comprises a remarkable set of enzymes that catalyze the hydrolysis of a wide range of substrates bearing amide or ester functional groups at carbon and phosphorus centers.
Journal ArticleDOI
Channeling of Substrates and Intermediates in Enzyme-Catalyzed Reactions
TL;DR: The three-dimensional structures of tryptophan synthase, carbamoyl phosphate Synthetase, glutamine phosphoribosylpyrophosphate amidotransferase, and asparagine synthetase have revealed the relative locations of multiple active sites within these proteins.
Journal ArticleDOI
Characterization of the zinc binding site of bacterial phosphotriesterase.
TL;DR: Protection against inactivation by metal chelation was afforded by the binding of competitive inhibitors, suggesting that at least one metal is at or near the active site.
Journal ArticleDOI
Structure of carbamoyl phosphate synthetase : a journey of 96 A from substrate to product
TL;DR: The two halves of the large subunit are related by a nearly exact 2-fold rotational axis, thus suggesting that this polypeptide chain evolved from a homodimeric precursor.