Information on EC 4.1.3.16 - 4-Hydroxy-2-oxoglutarate aldolase

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The expected taxonomic range for this enzyme is: Mammalia

EC NUMBER
COMMENTARY
4.1.3.16
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RECOMMENDED NAME
GeneOntology No.
4-Hydroxy-2-oxoglutarate aldolase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
condensation
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elimination
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of an oxo-acid, C-C bond cleavage
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PATHWAY
KEGG Link
MetaCyc Link
4-hydroxyproline degradation
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Arginine and proline metabolism
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Glyoxylate and dicarboxylate metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxy-2-oxoglutarate glyoxylate-lyase (pyruvate-forming)
The enzymes from rat liver and bovine liver act on both enantiomers of 4-hydroxy-2-oxoglutarate. cf. EC 4.1.3.42, L-4-hydroxy-2-oxoglutarate aldolase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-keto-4-hydroxybutyrate aldolase
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2-keto-4-hydroxyglutarate aldolase
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2-keto-4-hydroxyglutaric aldolase
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2-oxo-4-hydroxyglutarate aldolase
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2-oxo-4-hydroxyglutaric aldolase
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4-hydroxy-2-ketoglutarate aldolase
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4-hydroxy-2-ketoglutaric aldolase
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4-hydroxy-2-oxoglutarate aldolase
Q86XE5
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aldolase, 4-hydroxy-2-oxoglutarate
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DHDPSL
Q86XE5
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dihydrodipicolinate synthase-like enzyme
Q86XE5
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DL-4-Hydroxy-2-ketoglutarate aldolase
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EC 4.1.2.31
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formerly
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hOGA
Q86XE5
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hydroxyketoglutarate aldolase
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Hydroxyketoglutaric aldolase
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KHG-aldolase
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CAS REGISTRY NUMBER
COMMENTARY
9030-81-3
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
; bovine
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
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50 mM, enhances activity 2fold; activates kidney enzyme
KCl
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activates
additional information
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carboxylic acids activate
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TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
59
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constant decay of 0.011 1/min, slow inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
irreversibly inactivated by aminonitrile formation from cyanide and enzyme-substrate complex
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STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, Tris-HCl buffer, pH 7.4, 40% saturated with ammonium sulfate, 6 months, kidney enzyme
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4C, in either 50 mM Tris-HCl or potassium phosphate, pH 7.4, plus 5 mM 2-mercaptoethanol, 0.02% sodium azide, 40% saturated with ammonium sulfate, 100% of initial activity for at least 6 months
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4C, in either 50 mM Tris-HCl or potassium phosphate, pH 7.4, plus 5 mM 2-mercaptoethanol, 0.02% sodium azide, no substantial loss of enzymatic activity for up to 1 month
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5C, Tris-HCl buffer, pH 7.4, two weeks, sometimes several months
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