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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. .

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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.

HPD dioxygenates HPP

HPP + O2 → HGTA + CO2

Reactome: R-HSA-71163
Compartment: cytosol
Rhea: RHEA:16190

Inputs

HPPCHEBI:36242, C9H7O4, cytosol
O2CHEBI:15379, O2, cytosol

Outputs

HGTACHEBI:16169, C8H7O4, cytosol
CO2CHEBI:16526, CO2, cytosol

Catalysed by

4-hydroxyphenylpyruvate dioxygenase activity of HPD:AscH-:Fe2+ dimer [cytosol]EC 1.13.11.27

Literature

Mutations in the 4-hydroxyphenylpyruvate dioxygenase gene (HPD) in patients with tyrosinemia type III Hum Genet, 2000
The mechanism of enzymic formation of homogentisate from p-hydroxyphenylpyruvate J. Am. Chem. Soc., 1970
The genetic tyrosinemias Am J Med Genet C Semin Med Genet, 2006
Structure-based discovery of pyrazole-benzothiadiazole hybrid as human HPPD inhibitors Structure, 2023
Identification of key residues determining the binding specificity of human 4-hydroxyphenylpyruvate dioxygenase Eur J Pharm Sci, 2020
Functional role of residues involved in substrate binding of human 4-hydroxyphenylpyruvate dioxygenase Biochem J, 2021