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J. Biol. Chem., Vol. 275, Issue 45, 35646-35655, November 10, 2000
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From the Division of Nutritional Sciences, Cornell University,
Ithaca, New York 14853
We have identified and purified to homogeneity an
enzyme from rat liver that catalyzes the oxidative catabolism of
5-formyltetrahydrofolate to p-aminobenzoylglutamate
and a pterin derivative. Purification of the enzyme utilized six column
matrices, including a pterin-6-carboxylic acid affinity column.
Treatment of crude rat liver extracts with EDTA or heat decreased the
specific activity of the enzyme by up to 85%. Peptides generated from
the purified protein were sequenced and found to be identical to
primary sequences present within rat light chain or heavy chain
ferritin. Commercial rat ferritin did not display catabolic activity,
but activity could be acquired with iron loading. The purified enzyme
contained 2000 atoms of iron/ferritin 24-mer and displayed similar
electrophoretic properties as commercial rat liver ferritin. The
ferritin-catalyzed reaction displayed burst kinetics, and the enzyme
catalyzed only a single turnover in vitro. Expression of
rat heavy chain ferritin cDNA resulted in increased rates of folate
turnover in cultured Chinese hamster ovary cells and human mammary
carcinoma cells and reduced intracellular folate concentrations in
Chinese hamster ovary cells. These results indicate that ferritin
catalyzes folate turnover in vitro and in vivo
and may be an important factor in regulating intracellular folate concentrations.
Purification and Properties of a Folate-catabolizing Enzyme*
*
This work was supported in part by United States Public
Health Service Grant HD35678 (to P. J. S.) and Training Grant
DK07158-21 (to E. W. O. and J. R. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 607-255-9751;
Fax: 607-255-1033; E-mail: PJS13@cornell.edu.
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