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GAR + 10-Formyl-THF => FGAR + THF (R-HSA-73813) [Homo sapiens]

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Summation

The irreversible transfer of a formyl group to cytosolic 5-phosphoribosylglycinamide (GAR) to form 5'-phosphoribosylformylglycinamide (FGAR) is catalyzed by the phosphoribosylglycinamide formyltransferase domain of the trifunctional protein, "phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase" (GART) (Aimi et al. 1990; Zhang et al. 2002). Fluoresence microscopy studies of cultured human cells have shown that GART is cytosolic and suggest that it may co-localize with other enzymes of de novo IMP biosynthesis under some metabolic conditions (Gooljarsingh et al. 2001; An et al. 2008).

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Additional Information
Compartment cytosol
Components of this entry
Input entries
Output entries
Catalyst Activity
PhysicalEntity Activity Active Units
GART phosphoribosylglycinamide formyltransferase activity (0004644)  
Cross References
Database Identifier
Rhea 15056, 15054
Literature References
pubMedId Title Journal Year
2147474 De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-glycinamide ribonucleotide transformylase by functional complementation in E. coli Nucleic Acids Res 1990
12450384 Crystal structures of human GAR Tfase at low and high pH and with substrate beta-GAR Biochemistry 2002
11381136 Localization of GAR transformylase in Escherichia coli and mammalian cells Proc Natl Acad Sci USA 2001
18388293 Reversible compartmentalization of de novo purine biosynthetic complexes in living cells Science 2008
Inferred Entries
Orthologous events
 
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