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J. Biol. Chem., Vol. 265, Issue 24, 14227-14233, 08, 1990
P Stover and V Schirch
The combined activities of rabbit liver cytosolic serine
hydroxymethyltransferase and C1-tetrahydrofolate synthase convert
tetrahydrofolate and formate to 5-formyltetrahydrofolate. In this reaction
C1-tetrahydrofolate synthase converts tetrahydrofolate and formate to
5,10-methenyltetrahydrofolate, which is hydrolyzed to 5-
formyltetrahydrofolate by a serine hydroxymethyltransferase-glycine
complex. Serine hydroxymethyltransferase, in the presence of glycine,
catalyzes the conversion of chemically synthesized 5,10-
methenyltetrahydrofolate to 5-formyltetrahydrofolate with biphasic
kinetics. There is a rapid burst of product that has a half-life of
formation of 0.4 s followed by a slower phase with a completion time of
about 1 h. The substrate for the burst phase of the reaction was shown not
to be 5,10-methenyltetrahydrofolate but rather a one-carbon derivative of
tetrahydrofolate which exists in the presence of 5,10-
methenyltetrahydrofolate. This derivative is stable at pH 7 and is not an
intermediate in the hydrolysis of 5,10-methenyltetrahydrofolate to
10-formyltetrahydrofolate by C1-tetrahydrofolate synthase. Cytosolic serine
hydroxymethyltransferase catalyzes the hydrolysis of 5,10-
methenyltetrahydrofolate pentaglutamate to 5-formyltetrahydrofolate
pentaglutamate 15-fold faster than the hydrolysis of the monoglutamate
derivative. The pentaglutamate derivative of 5-formyltetrahydrofolate binds
tightly to serine hydroxymethyltransferase and dissociates slowly with a
half-life of 16 s. Both rabbit liver mitochondrial and Escherichia coli
serine hydroxymethyltransferase catalyze the conversion of
5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate at rates similar
to those observed for the cytosolic enzyme. Evidence that this reaction
accounts for the in vivo presence of 5- formyltetrahydrofolate is suggested
by the observation that mutant strains of E. coli, which lack serine
hydroxymethyltransferase activity, do not contain 5-formyltetrahydrofolate,
but both these cells, containing an overproducing plasmid of serine
hydroxymethyltransferase, and wild-type cells do have measurable amounts of
this form of the coenzyme.
Serine hydroxymethyltransferase catalyzes the hydrolysis of 5,10- methenyltetrahydrofolate to 5-formyltetrahydrofolate
Department of Biochemistry and Molecular Biophysics, Virginia Commonwealth University, Medical College of Virginia, Richmond 23298.
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