Article
A single site mutation can induce functional promiscuity in homoserine kinase.
Organic & biomolecular chemistry - 7 Jun 2023
Tripathi Ankita, Dubey Kshatresh Dutta
Abstract excerpt
L-Homoserine kinase is crucial in the biosynthesis of L-threonine, L-isoleucine, and L-methionine, where it catalyzes ATP-dependent phosphorylation of L-homoserine (Hse) to yield L-homoserine phosphate as its native activity. However, a single site mutation of H138 → L shows the emergence of ATPase activity as a secondary function. However, a previous mechanistic study proposes direct involvement of ATP and the...
Topics
- Phosphotransferases (Alcohol Group Acceptor)
- Homoserine
- Threonine
- Adenosine Triphosphate
- Mutation
- Adenosine Triphosphatases