Guanidoacetate methyltransferase. Purification and molecular properties.
Guanidoacetate methyltransferase has been purified about 140-fold from pig liver. Polyacrylamide gel electrophoresis of the purified enzyme showed four protein bands, each of which is associated with guanidoacetate methyltransferase activity. During gel electrophoresis at pH 3 in 8 M urea, guanidoacetate methyltransferase migrated as a single component. The molecular weight of the purified guanidoacetate methyltransferase was estimated to be 31,000 by sodium dodecyl sulfate-gel electrophoresis, which also showed only one protein component with guanidoacetate methyltransferase activity. This molecular weight is in agreement with that estimated by Sephadex G-75 chromatography. Guanidoacetate methyltransferase is inhibited by adenosylhomocysteine, 3-deazaadenosylhomocysteine, and sinefungin with Ki values of 16 microM, 39 microM, and 18 microM, respectively.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D006146:Guanidines; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008780:Methyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D012435:S-Adenosylhomocysteine / Q000494:pharmacology; D013552:Swine
D000596:Amino Acids; D006146:Guanidines; D012435:S-Adenosylhomocysteine; D008780:Methyltransferases