Article
A site-directed mutagenesis study on Escherichia coli inorganic pyrophosphatase. Glutamic acid-98 and lysine-104 are important for structural integrity, whereas aspartic acids-97 and -102 are essential for catalytic activity.
Biochemistry - 19 Jun 1990
Lahti R, Pohjanoksa K, Pitkäranta T, Heikinheimo P, Salminen T, Meyer P, Heinonen J
Abstract excerpt
Analysis of the conservation of functional residues between yeast and Escherichia coli inorganic pyrophosphatases (PPases) suggested that Asp-97, Glu-98, Asp-102, and Lys-104 are important for the action of E. coli PPase [Lahti, R., Kolakowski, L. F., Heinonen, J., Vihinen, M., Pohjanoksa, K., &...
Topics
- Amino Acid Sequence
- Aspartic Acid
- Base Sequence
- Binding Sites
- DNA, Bacterial
- Escherichia coli
- Glutamates
- Glutamic Acid
- Hot Temperature
- Inorganic Pyrophosphatase
- Lysine
- Molecular Sequence Data
- Mutation
- Pyrophosphatases