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Arabidopsis ITPK1 and ITPK2 Have an Evolutionarily Conserved Phytic Acid Kinase Activity
ACS chemical biology, 2019-10, Vol.14 (10), p.2127-2133
[Peer Reviewed Journal]
ISSN: 1554-8929 ;EISSN: 1554-8937 ;DOI: 10.1021/acschembio.9b00423 ;PMID: 31525024
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Title:
Arabidopsis ITPK1 and ITPK2 Have an Evolutionarily Conserved Phytic Acid Kinase Activity
Author:
Laha, Debabrata
;
Parvin, Nargis
;
Hofer, Alexandre
;
Giehl, Ricardo F. H
;
Fernandez-Rebollo, Nicolas
;
von Wirén, Nicolaus
;
Saiardi, Adolfo
;
Jessen, Henning J
;
Schaaf, Gabriel
Subjects:
Arabidopsis - enzymology
;
Arabidopsis Proteins - chemistry
;
Arabidopsis Proteins - genetics
;
Arabidopsis Proteins - isolation & purification
;
Enzyme Assays
;
Humans
;
Inositol Phosphates - biosynthesis
;
Oryza - enzymology
;
Phosphorylation
;
Phosphotransferases (Alcohol Group Acceptor) - chemistry
;
Phosphotransferases (Alcohol Group Acceptor) - genetics
;
Phosphotransferases (Alcohol Group Acceptor) - isolation & purification
;
Phytic Acid - chemistry
;
Saccharomyces cerevisiae - genetics
Is Part Of:
ACS chemical biology, 2019-10, Vol.14 (10), p.2127-2133
Description:
Diphospho-myo-inositol polyphosphates, also termed inositol pyrophosphates, are molecular messengers containing at least one high-energy phosphoanhydride bond and regulate a wide range of cellular processes in eukaryotes. While inositol pyrophosphates InsP7 and InsP8 are present in different plant species, both the identity of enzymes responsible for InsP7 synthesis and the isomer identity of plant InsP7 remain unknown. This study demonstrates that Arabidopsis ITPK1 and ITPK2 catalyze the phosphorylation of phytic acid (InsP6) to the symmetric InsP7 isomer 5-InsP7 and that the InsP6 kinase activity of ITPK enzymes is evolutionarily conserved from humans to plants. We also show by 31P nuclear magnetic resonance that plant InsP7 is structurally identical to the in vitro InsP6 kinase products of ITPK1 and ITPK2. Our findings lay the biochemical and genetic basis for uncovering physiological processes regulated by 5-InsP7 in plants.
Publisher:
United States: American Chemical Society
Language:
English
Identifier:
ISSN: 1554-8929
EISSN: 1554-8937
DOI: 10.1021/acschembio.9b00423
PMID: 31525024
Source:
Geneva Foundation Free Medical Journals at publisher websites
MEDLINE
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