Altering the Phosphorylation Position of Pyrophosphate-Dependent myo-Inositol-1-Kinase Based on Its Crystal Structure.

doi:10.1021/acschembio.0c00733

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Article

Altering the Phosphorylation Position of Pyrophosphate-Dependent myo-Inositol-1-Kinase Based on Its Crystal Structure.

ACS chemical biology - 21 May 2021

Tashiro Ryo, Sato Takaaki, Atomi Haruyuki, Miki Kunio, Fujihashi Masahiro

Abstract excerpt

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...

Topics

Catalytic Domain
Crystallization
Diphosphates
Inositol Phosphates
Kinetics
Magnetic Resonance Spectroscopy
Mutant Proteins
Mutation
Phosphoric Monoester Hydrolases
Phosphorylation
Protein Conformation
Tandem Mass Spectrometry
Thermotoga maritima

Source

Open in PubMed

Identifiers

PMID: 33877806
DOI: 10.1021/acschembio.0c00733

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