Article
Functional role of the amino-terminal mobile segment in catalysis by porcine cytosolic aspartate aminotransferase. Critical importance of Val17 and Phe18 for productive binding of substrates.
The Journal of biological chemistry - 7 Oct 1994
Nishimura K, Higaki T, Okamura H, Tanase S
Abstract excerpt
A notable feature of porcine cytosolic aspartate aminotransferase is the closure of the active site cleft by a mobile amino-terminal segment (residues 15-40) upon binding substrate. The functional roles of Val17 and Phe18, residues that are part of the mobile loop, have been studied in the site-directed mutants in which the size and hydrophobic nature of these residues have been changed. Absorption, circular...
Topics
- Animals
- Aspartate Aminotransferases
- Base Sequence
- Cytosol
- Kinetics
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Mutation
- Phenylalanine
- Structure-Activity Relationship