Structural highlights
Function
Q9WYP6_THEMA
Publication Abstract from PubMed
Most kinases utilize ATP as a phosphate donor and phosphorylate a wide range of phosphate acceptors. An alternative phosphate donor is inorganic pyrophosphate (PPi), which costs only 1/1000 of ATP. To develop a method to engineer PPi-dependent kinases, we herein aimed to alter the product of PPi-dependent myo-inositol kinase from d-myo-inositol 1-phosphate to d-myo-inositol 3-phosphate. For this purpose, we introduced the myo-inositol recognition residues of the ATP-dependent myo-inositol-3-kinase into the PPi-dependent myo-inositol-1-kinase. This replacement was expected to change the 3D arrangements of myo-inositol in the active site and bring the hydroxyl group at the 3C position close to the catalytic residue. LC-MS and NMR analyses proved that the engineered enzyme successfully produced myo-inositol 3-phosphate from PPi and myo-inositol.
Altering the Phosphorylation Position of Pyrophosphate-Dependent myo-Inositol-1-Kinase Based on Its Crystal Structure.,Tashiro R, Sato T, Atomi H, Miki K, Fujihashi M ACS Chem Biol. 2021 Apr 20. doi: 10.1021/acschembio.0c00733. PMID:33877806[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tashiro R, Sato T, Atomi H, Miki K, Fujihashi M. Altering the Phosphorylation Position of Pyrophosphate-Dependent myo-Inositol-1-Kinase Based on Its Crystal Structure. ACS Chem Biol. 2021 Apr 20. doi: 10.1021/acschembio.0c00733. PMID:33877806 doi:http://dx.doi.org/10.1021/acschembio.0c00733
