HOGA1 tetramer aldol-cleaves 4-OH-2-oxoglutarate (HOG) to glyoxylate and pyruvate

Stable Identifier
R-HSA-6784423
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Mitochondrial HOGA1 aldol-cleaves 4-OH-2-oxoglutarate (HOG) to glyoxylate and pyruvate. The biochemical details of the enzyme are inferred from the properties of its well-studied rat homologue (Maitra & Dekker 1964). The mature protein lacks a 25-residue mitochondrial targeting sequence and forms a homotetramer (Riedel et al. 2011).

Literature References
PubMed ID Title Journal Year
21998747 Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria

Knight, J, Holmes, RP, Hantgan, RR, Johnson, LC, Riedel, TJ, Lowther, WT

PLoS ONE 2011
14193832 Purification and properties of rat liver 2-keto-4-hydroxyglutarate aldolase

Maitra, U, Dekker, EE

J. Biol. Chem. 1964
Participants
Participates
Event Information
Catalyst Activity

4-hydroxy-2-oxoglutarate aldolase activity of HOGA1 tetramer [mitochondrial matrix]

Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created
Cite Us!