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

Liliane Assairi, Gilles Labesse, Dominique Douguet, Anne Marie Gilles

Journal: Trends in biochemical sciences 2002;27(6):273-5

PMID: 12069781

Full Text on Elsevier Science View on PubMed

Abstract

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.

Address: Centre de Biochimie Structurale, INSERM U554-CNRS UMR5048, Universite Montpellier I, 15 Avenue Charles Flahault, 34060 Montpellier Cedex, France. [email protected]

DOI: 10.1016/s0968-0004(02)02093-5

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MeSH Terms: Allosteric Site, Amino Acid Motifs, Amino Acid Sequence, Diacylglycerol Kinase, Molecular Sequence Data, Phosphofructokinase-1, Phosphorylation, Phosphotransferases (Alcohol Group Acceptor)