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Diversification in the inositol tris/tetrakisphosphate kinase (ITPK) family: crystal structure and enzymology of the outlier AtITPK4

Abstract:

Myo-inositol tris/tetrakisphosphate kinases (ITPKs) catalyze diverse phosphotransfer reactions with myo-inositol phosphate and myo-inositol pyrophosphate substrates. However, the lack of structures of nucleotide-coordinated plant ITPKs thwarts a rational understanding of phosphotransfer reactions of the family. Arabidopsis possesses a family of four ITPKs of which two isoforms, ITPK1 and ITPK4, control inositol hexakisphosphate and inositol pyrophosphate levels directly or by provision of pre...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1042/BCJ20220579

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Pharmacology
Oxford college:
University College
Role:
Author
ORCID:
0000-0003-3255-9135
et al.
Publisher:
Portland Press
Journal:
Biochemical Journal More from this journal
Volume:
480
Pages:
433–453
Publication date:
2023-03-29
Acceptance date:
2023-03-10
DOI:
EISSN:
1470-8728
ISSN:
0264-6021
Language:
English
Keywords:
Pubs id:
1333391
Local pid:
pubs:1333391
Deposit date:
2023-03-20

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