Rat guanidinoacetate methyltransferase: mutation of amino acids within a common sequence motif of mammalian methyltransferase does not affect catalytic activity but alters proteolytic susceptibility.
1. Manual alignment of amino acid sequences of mammalian S-adenosylmethionine-dependent methyltransferases of known sequence revealed the presence of 2 homologous regions. 2. The sequence of the region at the C-terminal side is unique to mammalian methyltransferases, and in guanidinoacetate methyltransferase this sequence occurs at residues 159-165. 3. Mutagenesis of 5 conserved residues in this sequence did not affect the catalytic activity but altered tryptic susceptibility at Arg20.
Gomi
T
T
Department of Biochemistry, Toyama Medical and Pharmaceutical University Faculty of Medicine, Japan.
Tanihara
K
K
Date
T
T
Fujioka
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002384:Catalysis; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D050937:Guanidinoacetate N-Methyltransferase; D006358:Hot Temperature; D006868:Hydrolysis; D008780:Methyltransferases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D051381:Rats; D012436:S-Adenosylmethionine / Q000378:metabolism; D016415:Sequence Alignment
D012436:S-Adenosylmethionine; D008780:Methyltransferases; C494508:Gamt protein, rat; D050937:Guanidinoacetate N-Methyltransferase