Note: a dashed line (without arrowheads) between two compound names is meant to imply that the two names are just different instantiations of the same compound -- i.e. one may be a specific name and the other a general name, or they may both represent the same compound in different stages of a polymerization-type pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
|Superclasses:||Biosynthesis → Cofactors, Prosthetic Groups, Electron Carriers Biosynthesis → Vitamins Biosynthesis → Folate Biosynthesis|
Pathway Summary from MetaCyc:
Folates are tripartite molecules comprising pterin, p-aminobenzoate (pABA), and glutamate moieties. In natural folates the pterin ring exists in the dihydro or tetrahydro state. Folate usually has a gamma-linked polyglutamyl tail of up to eight residues attached to the first glutamate. The one-carbon units (methyl or formyl) are either attached to the N-5 of the pterin moiety, to the N-10 of the pABA moiety or bridged in between these two (e.g., 5,10-methenyl or methylene-THF). 10-formyl-tetrahydrofolates are involved in tetrahydrofolate, purine and formate synthesis [Nagy95, deCrecyLagard07].
About This Pathway
The formation of the formyl and methyl derivatives of tetrahydrofolate (vitamin B9) directly involved in or representing sidesteps of the biosynthesis of this vital cofactor is displayed in this pathway. Conversion of 10-formyl-tetrahydrofolate to tetrahydrofolate occurs either directly through hydrolysis or via 5-methyl-tetrahydrofolate in several steps [Nagy95, deCrecyLagard07].
Variants: 4-aminobenzoate biosynthesis, folate polyglutamylation, superpathway of tetrahydrofolate biosynthesis, superpathway of tetrahydrofolate biosynthesis and salvage, tetrahydrofolate biosynthesis, tetrahydrofolate salvage from 5,10-methenyltetrahydrofolate
Pathway Evidence Glyph:
This organism is in the expected taxonomic range for this pathway.
Key to pathway glyph edge colors:
An enzyme catalyzing this reaction is present in this organism
No enzyme catalyzing this reaction has been identified in this organism
The reaction is unique to this pathway in MetaCyc
deCrecyLagard07: de Crecy-Lagard V, El Yacoubi B, de la Garza RD, Noiriel A, Hanson AD (2007). "Comparative genomics of bacterial and plant folate synthesis and salvage: predictions and validations." BMC Genomics 8;245. PMID: 17645794
Nagy95: Nagy PL, Marolewski A, Benkovic SJ, Zalkin H (1995). "Formyltetrahydrofolate hydrolase, a regulatory enzyme that functions to balance pools of tetrahydrofolate and one-carbon tetrahydrofolate adducts in Escherichia coli." J Bacteriol 1995;177(5);1292-8. PMID: 7868604
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493