Methylenetetrahydrofolate dehydrogenase – methenyltetrahydrofolate cyclohydrolase – formyltetrahydrofolate synthetase from porcine liver Location of the activities in two domains of the multifunctional polypeptide

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Abstract
Chymotryptic cleavage of the trifunctional protein methylenetetrahydrofolate-dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase from pig liver yields a fragment of 2/3 the original polypeptide that retains only synthetase activity. A smaller polypeptide corresponding to .apprx. 1/3 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 2 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.

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