A dimeric creatine kinase from a sponge: implications in terms of phosphagen kinase evolution.
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.
Ellington
W R
WR
Department of Biological Science, Florida State University, Tallahassee 32306-4370, USA. elling@bio.fsu.edu
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
D017852:Phosphotransferases (Nitrogenous Group Acceptor); C023839:glycocyamine phosphokinase; D003402:Creatine Kinase; D001122:Arginine Kinase; C021517:lombricine kinase