Article
Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant.
Biochemistry - 7 Mar 1995
Kallarakal A T, Mitra B, Kozarich J W, Gerlt J A, Clifton J G, Petsko G A, Kenyon G L
Abstract excerpt
On the basis of the available high-resolution structures of mandelate racemase (MR) from Pseudomonas putida [Landro, J. A., Gerlt, J. A., Kozarich, J. W., Koo, C. W., Shah, V. J., Kenyon, G. L., Neidhart, D. J., Fujita, J., & Petsko, G. A. (1994) Biochemistry 33, 635-643], Lys 166 and His 297 are positioned appropriately to participate in catalysis as acid/base catalysts that either abstract the alpha-proton from...
Topics
- Base Sequence
- Binding Sites
- Catalysis
- Crystallography, X-Ray
- DNA, Bacterial
- Escherichia coli
- Kinetics
- Mandelic Acids
- Models, Molecular
- Molecular Sequence Data
- Molecular Structure