Article
Structural role of a conserved active site cis proline in the Thermotoga maritima acetyl esterase from the carbohydrate esterase family 7.
Proteins - 1 Apr 2017
Singh Mrityunjay K, Manoj Narayanan
Abstract excerpt
A conserved cis proline residue located in the active site of Thermotoga maritima acetyl esterase (TmAcE) from the carbohydrate esterase family 7 (CE7) has been substituted by alanine. The residue was known to play a crucial role in determining the catalytic properties of the enzyme. To elucidate the structural role of the residue, the crystal structure of the Pro228Ala variant (TmAcEP228A ) was determined at 2.1...
Topics
- Acetylesterase
- Alanine
- Amino Acid Sequence
- Amino Acid Substitution
- Bacterial Proteins
- Binding Sites
- Biocatalysis
- Catalytic Domain
- Cloning, Molecular
- Crystallography, X-Ray
- Escherichia coli
- Gene Expression
- Kinetics
- Models, Molecular