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DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap

Data

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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

Select a territory to bring it forward.

Reading the map

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.

PPT1 hydrolyses palmitoylated proteins

PALM:protein + H2O → PALM + protein + H+

Reactome: R-HSA-5690517
Compartment: lysosomal lumen
Rhea: RHEA:19234

Inputs

PALM:proteinR-ALL-5690533, lysosomal lumen
H2OCHEBI:15377, H2O, lysosomal lumen

Outputs

PALMCHEBI:7896, C16H31O2, lysosomal lumen
proteinCHEBI:36080, lysosomal lumen
H+CHEBI:15378, H, lysosomal lumen

Catalysed by

palmitoyl-(protein) hydrolase activity of PPT1 [lysosomal lumen]EC 3.1.2.22; UniProt P50897

Literature

New players on the metabolic stage: How do you like Them Acots? Adipocyte, 2013
The emerging role of acyl-CoA thioesterases and acyltransferases in regulating peroxisomal lipid metabolism Biochim. Biophys. Acta, 2012
Functional and structural properties of mammalian acyl-coenzyme A thioesterases Prog. Lipid Res., 2010
Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras J. Biol. Chem., 1993
Molecular cloning and expression of palmitoyl-protein thioesterase J. Biol. Chem., 1994