Bennett Lab - Payam Mehrshahi

Tetrahydrofolate (THF) functions as substrates and coenzymes in single
carbon transfer reactions necessary to synthesise components of DNA,
RNA, and proteins. Humans lack the complete folate biosynthetic pathway
and thus rely on dietary intake to meet their requirements. A
significant proportion of THF is polyglutamylated, a process catalyzed
by folylpolyglutamate synthetase (FPGS), which adds glutamate residues
to the para-aminobenzoate moiety.
In plants, the polyglutamate chain is the principal means by which THF
is retained and is compartmentalised within cells. Furthermore,
polyglutamated THF are the preferred substrates for enzymes such as
methionine synthase, serine hydroxymethyltransferase and thymidylate
synthase (Ravanel et al., 2004; Huang et al., 1998; Kamb et al., 1992).

The objectives of this study have been to systematically explore the
role of THF polyglutamylation on one-carbon metabolism and plant
development.

- Nutritional genomics page.

References:
Kamb et al (1992) Biochemistry 31: 9883-9890.
Ravanel et al (2001) PNAS 98: 15360-15365.
Ravanel et al (2004) J. Biol. Chem. 279: 22548-22557.

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