Title : Regulation of folate and one-carbon metabolism in mammalian cells. I. Folate metabolism in Chinese hamster ovary cells expressing Escherichia coli or human folylpoly-gamma-glutamate synthetase activity.

Pub. Date : 1993 Oct 15

PMID : 8408018






8 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Folate metabolism in Chinese hamster ovary cells expressing Escherichia coli or human folylpoly-gamma-glutamate synthetase activity. Folic Acid folylpolyglutamate synthase Homo sapiens
2 Only low levels of FPGS are required to enable cellular metabolism of folates to forms that are retained by mammalian cells. Folic Acid folylpolyglutamate synthase Homo sapiens
3 At low medium folate concentrations, folate accumulation by transfectants expressing human FPGS was not responsive to FPGS levels as the limiting step in metabolism was beyond the triglutamate, the chain length required for retention. Folic Acid folylpolyglutamate synthase Homo sapiens
4 The rate-limiting step in folate metabolism in cells expressing the E. coli enzyme was the conversion of diglutamate to triglutamate, and, at low FPGS levels, the E. coli enzyme was about 50-fold less effective than the human FPGS in enabling cellular folate accumulation. Folic Acid folylpolyglutamate synthase Homo sapiens
5 The rate-limiting step in folate metabolism in cells expressing the E. coli enzyme was the conversion of diglutamate to triglutamate, and, at low FPGS levels, the E. coli enzyme was about 50-fold less effective than the human FPGS in enabling cellular folate accumulation. Folic Acid folylpolyglutamate synthase Homo sapiens
6 The rate-limiting step in folate metabolism in cells expressing the E. coli enzyme was the conversion of diglutamate to triglutamate, and, at low FPGS levels, the E. coli enzyme was about 50-fold less effective than the human FPGS in enabling cellular folate accumulation. Folic Acid folylpolyglutamate synthase Homo sapiens
7 These data suggest that cellular accumulation of any folate analog whose mono- or diglutamate derivative is a poor substrate for FPGS would be very responsive to the level of FPGS activity. Folic Acid folylpolyglutamate synthase Homo sapiens
8 These data suggest that cellular accumulation of any folate analog whose mono- or diglutamate derivative is a poor substrate for FPGS would be very responsive to the level of FPGS activity. Folic Acid folylpolyglutamate synthase Homo sapiens