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DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap

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Human metabolism

Reactome's human metabolism drawn as one network. Each molecule has one home node; widely shared molecules also appear as dashed copies in other territories, linked from their details. .

Territories

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Metabolite; its structure appears as you zoom in
Reaction, arrow toward the product
Cofactors and co-substrates are written beside the reaction when you zoom in
Dashed ring: a copy of a widely shared molecule or cofactor in another territory or pathway
Compartment transfer of the molecule it is linked to
Binding, release or complex event; its proteins are named in its details
Outline: reactions mostly in the mitochondrion

Arrows follow Reactome's curated reaction direction.

5-phospho-alpha-D-ribose 1-diphosphate (PRPP) + H2O + L-glutamine 5-phosphoribosylamine + L-glutamate +pyrophosphate

PRPP + L-Gln + H2O → PRA + L-Glu + PPi

Reactome: R-HSA-73815
Compartment: cytosol
Rhea: RHEA:14907

Inputs

PRPPCHEBI:58017, C5H8O14P3, cytosol
L-GlnCHEBI:58359, C5H10N2O3, cytosol
H2OCHEBI:15377, H2O, cytosol

Outputs

PRACHEBI:58681, C5H11NO7P, cytosol
L-GluCHEBI:29985, C5H8NO4, cytosol
PPiCHEBI:33019, HO7P2, cytosol

Catalysed by

amidophosphoribosyltransferase activity of PPAT dimer [cytosol]EC 2.4.2.14

Literature

Human glutamine phosphoribosylpyrophosphate amidotransferase. Kinetic and regulatory properties J Biol Chem, 1973
Human glutamine phosphoribosylpyrophosphate amidotransferase. Two molecular forms interconvertible by purine ribonucleotides and phosphoribosylpyrophosphate J Biol Chem, 1973
Human amidophosphoribosyltransferase. An oxygen-sensitive iron-sulfur protein J Biol Chem, 1979
Molecular cloning of human amidophosphoribosyltransferase Biochem Biophys Res Commun, 1993
Reversible compartmentalization of de novo purine biosynthetic complexes in living cells Science, 2008