title: Purification and properties of the Hpa I methylase.
abstract: The purification and catalytic properties of the homogeneous Hpa I methylase is described. The enzyme exists as a single polypeptide chain with a molecular weight of 37,000 +/- 2,000 was shown by sedimentation equilibrium and polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The Hpa I methylase transfers methyl groups of S-adenosylmethionine to adenine present in the recognition sequence d(G-T-T-A-A*-C), A* is the N6 methyl adenosine. An average of 2.1 methyl groups per recognition site are transferred by the Hpa I methylase.
mesh_terms: D006193:Haemophilus influenzae / Q000201:enzymology*; D007700:Kinetics; D008780:Methyltransferases / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D012436:S-Adenosylmethionine; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific); D013379:Substrate Specificity
chemical_list: D012436:S-Adenosylmethionine; C036341:DNA modification methylase HpaI; D008780:Methyltransferases; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific)