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Diacylglyceride kinases, sphingosine kinases and NAD kinases: distant relatives of 6-phosphofructokinases

Authors :
Liliane Assairi
Anne-Marie Gilles
Gilles Labesse
Dominique Douguet
Centre de Biochimie Structurale [Montpellier] (CBS)
Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM)
Chimie Structurale des Macromolécules (CSM)
Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)
Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)
Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)
Source :
Trends in Biochemical Sciences, Trends in Biochemical Sciences, Elsevier, 2002, 27 (6), pp.273-275. ⟨10.1016/S0968-0004(02)02093-5⟩, Trends in Biochemical Sciences, 2002, 27 (6), pp.273-275. ⟨10.1016/S0968-0004(02)02093-5⟩
Publication Year :
2002
Publisher :
HAL CCSD, 2002.

Abstract

International audience; Diacylglyceride kinases, sphingosine kinases, NAD kinases and 6-phosphofructokinases are thought to be related despite large evolution of their sequences. Discovery of a common signature has led to the suggestion that they possess a similar phosphate-donor-binding site and a similar phosphorylation mechanism. The substrate- and allosteric-binding sites are much more divergent and their delineation remains to be determined experimentally.

Details

Language :
English
ISSN :
09680004
Database :
OpenAIRE
Journal :
Trends in Biochemical Sciences, Trends in Biochemical Sciences, Elsevier, 2002, 27 (6), pp.273-275. ⟨10.1016/S0968-0004(02)02093-5⟩, Trends in Biochemical Sciences, 2002, 27 (6), pp.273-275. ⟨10.1016/S0968-0004(02)02093-5⟩
Accession number :
edsair.doi.dedup.....4a18cb4b9de2a220ac3fc549ff715465
Full Text :
https://doi.org/10.1016/S0968-0004(02)02093-5⟩