title: A dimeric creatine kinase from a sponge: implications in terms of phosphagen kinase evolution.
abstract: This study demonstrates conclusively that tissues of the sponge Tethya aurantia contain significant creatine kinase (CK) activity. This CK was purified and analyzed with respect to a number of physico-chemical properties. Size exclusion chromatography and denaturing gel electrophoresis analyses showed that this enzyme is dimeric. The sequences of several Lys-C endoproteinase peptides from Tethya CK are consistent with this enzyme being a member of the phosphagen kinase family and a true CK. CK in higher organisms exists in a variety of quaternary structure forms--dimer, octamer and large monomer consisting of a three contiguous CK domains. The present results indicate that CK evolved very early in metazoan evolution and that the dimeric structure preceded other subunit association forms.
authors.affiliation: Department of Biological Science, Florida State University, Tallahassee 32306-4370, USA. elling@bio.fsu.edu
authors.forename: W R
authors.initials: WR
authors.lastname: Ellington
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001122:Arginine Kinase / Q000032:analysis* / Q000302:isolation & purification; D003402:Creatine Kinase / Q000032:analysis* / Q000145:classification / Q000302:isolation & purification; D019281:Dimerization; D019143:Evolution, Molecular; D006801:Humans; D008969:Molecular Sequence Data; D017852:Phosphotransferases (Nitrogenous Group Acceptor) / Q000032:analysis* / Q000302:isolation & purification; D011161:Porifera / Q000201:enzymology*; D012621:Seasons; D017386:Sequence Homology, Amino Acid
chemical_list: D017852:Phosphotransferases (Nitrogenous Group Acceptor); C023839:glycocyamine phosphokinase; D003402:Creatine Kinase; D001122:Arginine Kinase; C021517:lombricine kinase