Diacylglyceride kinases, sphingosine kinases and NAD kinases: distant relatives of 6-phosphofructokinases.
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.
Labesse
Gilles
G
Centre de Biochimie Structurale, INSERM U554-CNRS UMR5048, Universite Montpellier I, 15 Avenue Charles Flahault, 34060 Montpellier Cedex, France. labesse@cbs.cnrs.fr
Douguet
Dominique
D
Assairi
Liliane
L
Gilles
Anne Marie
AM
D000495:Allosteric Site; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D019852:Diacylglycerol Kinase / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D010732:Phosphofructokinase-1 / Q000737:chemistry* / Q000378:metabolism; D010766:Phosphorylation; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry* / Q000378:metabolism; D000099157:Sphingosine Kinase
D019852:Diacylglycerol Kinase; D010732:Phosphofructokinase-1; D017853:Phosphotransferases (Alcohol Group Acceptor); D000099157:Sphingosine Kinase; C021844:NAD kinase