Article
Quenching of the amidolytic activity of one-chain tissue-type plasminogen activator by mutation of lysine-416.
Biochemistry - 10 Apr 1990
Petersen L C, Boel E, Johannessen M, Foster D
Abstract excerpt
In contrast to most other serine proteases, tissue-type plasminogen activator (t-PA) possesses enzymatic activity as the one-chain zymogen form. The hypothesis that lysine residues 277 or 416 may be involved in stabilization of an active conformation of one-chain t-PA via salt-bridge formation with aspartic acid residue 477 was tested by site-directed mutagenesis. Four recombinant t-PA mutants were constructed....
Topics
- Amidohydrolases
- Base Sequence
- Binding Sites
- Cloning, Molecular
- Fibrin
- Humans
- Kinetics
- Lysine
- Macromolecular Substances
- Molecular Sequence Data
- Mutation
- Sequence Homology, Nucleic Acid