Chemistry:10-Formyltetrahydrofolate
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| Preferred IUPAC name
(2S)-2-[4-(N-{[(6Ξ)-2-Amino-4-oxo-1,4,5,6,7,8-hexahydropteridin-6-yl]methyl}formamido)benzamido]pentanedioic acid | |
Other names
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3D model (JSmol)
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| MeSH | 10-formyl-tetrahydrofolate |
PubChem CID
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| Properties | |
| C20H23N7O7 | |
| Molar mass | 473.44 g/mol |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). | |
 verify (what is   ?)
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| Infobox references | |
10-Formyltetrahydrofolate (10-CHO-THF) is a form of tetrahydrofolate that acts as a donor of formyl groups in anabolism. In these reactions 10-CHO-THF is used as a substrate in formyltransferase reactions.
Functions
Two equivalents of 10-CHO-THF are required in purine biosynthesis through the pentose phosphate pathway, where 10-CHO-THF is a substrate for phosphoribosylaminoimidazolecarboxamide formyltransferase.
10-CHO-THF is required for the formylation of methionyl-tRNA formyltransferase to give fMet-tRNA.[1]
Formation from methenyltetrahydrofolate
10-CHO-THF is produced from methylenetetrahydrofolate (CH2H4F) via a two step process. The first step generates 5,10-methenyltetrahydrofolate:[2]
- CH2H4F + NAD+ [math]\displaystyle{ \rightleftharpoons }[/math] CH2H2F + NADH + H+
In the second step 5,10-methenyltetrahydrofolate undergoes hydrolysis:
- CH2H2F + H2O [math]\displaystyle{ \rightleftharpoons }[/math] CHO-H4F +
The latter is equivalently written:
- 5,10-methenyltetrahydrofolate + H2O [math]\displaystyle{ \rightleftharpoons }[/math] 10-formyltetrahydrofolate
10-CHO-THF is also produced by the reaction
- ATP + formate + tetrahydrofolate [math]\displaystyle{ \rightleftharpoons }[/math] ADP + phosphate + 10-formyltetrahydrofolate
This reaction is catalyzed by formate-tetrahydrofolate ligase.
It can be converted back into tetrahydrofolate (THF) by formyltetrahydrofolate dehydrogenase or THF and formate by formyltetrahydrofolate deformylase.
References
- ↑ Voet, Donald (2016). Fundamentals of Biochemistry: Life at the Molecular Level (5th ed.). Wiley. pp. 1006–1007. ISBN 978-1-118-91840-1.
- ↑ Peter D. Pawelek; Robert E. MacKenzie (1998). "Methenyltetrahydrofolate Cyclohydrolase Is Rate Limiting for the Enzymatic Conversion of 10-Formyltetrahydrofolate to 5,10-Methylenetetrahydrofolate in Bifunctional Dehydrogenase-Cyclohydrolase Enzymes". Biochemistry 37 (4): 1109–1115. doi:10.1021/bi971906t. PMID 9454603.
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