Methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase from porcine liver. Location of the activities in two domains of the multifunctional polypeptide.
Chymotryptic cleavage of the trifunctional protein methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase from pig liver yields a fragment of two-thirds the original polypeptide that retains only synthetase activity. A smaller polypeptide corresponding to about one-third of the original polypeptide was shown earlier to retain dehydrogenase-cyclohydrolase activity. On immunodiffusion, the synthetase fragment cross-reacts and shows partial identity with antibodies raised against the uncleaved enzyme but shows nonidentity with the dehydrogenase-cyclohydrolase fragment, suggesting that the two fragments are derived from different regions of the polypeptide. Amino-terminal analysis of the peptides and uncleaved enzyme indicate that the dehydrogenase-cyclohydrolase activities are located at the amino-terminal region and the synthetase near the carboxyl-terminal portion of the polypeptide.
D000595:Amino Acid Sequence; D000619:Aminohydrolases / Q000378:metabolism*; D000818:Animals; D005574:Formate-Tetrahydrofolate Ligase / Q000032:analysis / Q000378:metabolism*; D008025:Ligases / Q000378:metabolism*; D008754:Methylenetetrahydrofolate Dehydrogenase (NADP) / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism*; D013763:Tetrahydrofolates / Q000378:metabolism
D009097:Multienzyme Complexes; D013763:Tetrahydrofolates; D010088:Oxidoreductases; D008754:Methylenetetrahydrofolate Dehydrogenase (NADP); D000619:Aminohydrolases; D008025:Ligases; D005574:Formate-Tetrahydrofolate Ligase