|PROSITE documentation PDOC00616 [for PROSITE entry PS00766]|
Enzymes that participate in the transfer of one-carbon units are involved in various biosynthetic pathways. In many of these processes the transfers of one-carbon units are mediated by the coenzyme tetrahydrofolate (THF). Various reactions generate one-carbon derivatives of THF which can be interconverted between different oxidation states by formyltetrahydrofolate synthetase (EC 188.8.131.52), methylenetetrahydrofolate dehydrogenase (EC 184.108.40.206 or EC 220.127.116.11) and methenyltetrahydrofolate cyclohydrolase (EC 18.104.22.168).
The dehydrogenase and cyclohydrolase activities are expressed by a variety of multifunctional enzymes:
The sequence of the dehydrogenase/cyclohydrolase domain is highly conserved in all forms of the enzyme. As signature patterns we selected two conserved regions. The first one is located in the N-terminal part of these enzymes and contains three acidic residues. The second pattern is a highly conserved sequence of 9 amino acids which is located in the C-terminal section.Last update:
December 2004 / Patterns and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Shannon K.W. Rabinowitz J.C.|
|Title||Isolation and characterization of the Saccharomyces cerevisiae MIS1 gene encoding mitochondrial C1-tetrahydrofolate synthase.|
|Source||J. Biol. Chem. 263:7717-7725(1988).|
|2||Authors||Belanger C. MacKenzie R.E.|
|Title||Isolation and characterization of cDNA clones encoding the murine NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase.|
|Source||J. Biol. Chem. 264:4837-4843(1989).|
|3||Authors||d'Ari L. Rabinowitz J.C.|
|Source||J. Biol. Chem. 266:23953-23958(1991).|