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Information on EC 4.1.3.16 - 4-Hydroxy-2-oxoglutarate aldolase
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4.1.3.16 4-Hydroxy-2-oxoglutarate aldolaseIUBMB Comments
The enzymes from rat liver and bovine liver act on both enantiomers of 4-hydroxy-2-oxoglutarate. cf. EC 4.1.3.42, (4S)-4-hydroxy-2-oxoglutarate aldolase.
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Word Map
- 4.1.3.16
- hyperoxalurias
- oxalate
-
stone
- ph2
- grhpr
- hydroxyproline
- urolithiasis
- 2-keto-3-deoxy-6-phosphogluconate
-
nephrocalcinosis
-
alanine-glyoxylate
-
nephrolithiasis
- synthesis
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
hoga1, 4-hydroxy-2-oxoglutarate aldolase, 2-keto-4-hydroxyglutarate aldolase, 2-oxo-4-hydroxyglutarate aldolase, dhdpsl, 4-hydroxy-2-ketoglutarate aldolase, entner-doudoroff aldolase, dihydrodipicolinate synthase-like enzyme, 
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SYNONYM 
ORGANISM
UNIPROT
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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-
-
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2-oxo-4-hydroxyglutarate aldolase
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-
-
-
2-oxo-4-hydroxyglutaric aldolase
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-
-
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4-hydroxy-2-ketoglutarate aldolase
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-
-
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4-hydroxy-2-ketoglutaric aldolase
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-
-
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aldolase, 4-hydroxy-2-oxoglutarate
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-
-
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DL-4-Hydroxy-2-ketoglutarate aldolase
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-
-
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EC 4.1.2.1
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formerly
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EC 4.1.2.31
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formerly
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hOGA
HOGA1
hydroxyketoglutarate aldolase
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-
-
-
Hydroxyketoglutaric aldolase
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-
-
-
KHG-aldolase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
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 SOURCE
PATHWAYS
BRENDA
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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, (4S)-4-hydroxy-2-oxoglutarate aldolase.
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CAS REGISTRY NUMBER
COMMENTARY
9030-81-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-hydroxy-2-oxoglutarate
?
-
catabolism of hydroxyproline, condensation physiologically less important
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-
?
Glyoxylate + pyruvate
4-Hydroxy-2-ketoglutarate
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higher specificity for pyruvate than for glyoxylate
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-
?
Glyoxylate + pyruvate
4-Hydroxy-2-ketoglutarate
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specific, codensation favoured, Keq: 0.73 mM
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?
Glyoxylate + pyruvate
4-Hydroxy-2-ketoglutarate
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3-substituted analogs
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-
?
Oxaloacetate
CO2 + pyruvate
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beta-decarboxylation, about 50% as effective as aldolase
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?
additional information
?
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functional role of SH-groups, conformational changes during catalysis
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-
?
additional information
?
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-
2-keto-4-hydroxy-4-methylglutarate, 2-keto-3-deoxy-6-phosphoclucanate cleaved at slow rate
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-
?
additional information
?
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-
2-keto-3-deoxyglucarate and 2-keto-4,5-dihydroxyvalerate cleaved at slow rate
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-
?
additional information
?
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enzyme shows no stereospecificity in catalyzing the aldol cleavage of the two optical isomers of 2-keto-4-hydroxyglutarate. Enzyme also catalyzes the beta-decarboxylation of oxalacetate, its decarboxylase/aldolae activity ratio is lower than that seen with the pure enzyme from either bovine liver or Escherichia coli
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-
?
additional information
?
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enzyme performs a retro-aldol cleavage reaction reminiscent of the trimeric 2-keto-3-deoxy-6-phosphogluconate aldolases
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-
?
additional information
?
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enzyme performs a retro-aldol cleavage reaction reminiscent of the trimeric 2-keto-3-deoxy-6-phosphogluconate aldolases
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-
?
additional information
?
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equilibrium favours condensation, Keq: 0.73 1/mM
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-
?
additional information
?
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2-keto-3-deoxyglucarate and 2-keto-4,5-dihydroxyvalerate cleaved at slow rate
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-hydroxy-2-oxoglutarate
?
-
catabolism of hydroxyproline, condensation physiologically less important
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-Ketobutyrate
-
competitive, Ki for 2-keto-4-hydroxybutyrate cleavage: 53 mM, Ki for 2-keto-4-hydroxyglutarate cleavage: 52 mM
CN-
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irreversible, in presence of aldehydes, reversible in abscence of aldehydes, 2-keto-4-hydroxyglutarate cleavage, Ki: 0.57 mM
glycolaldehyde
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competitive, Ki for 2-keto-4-hydroxybutyrate cleavage: 2.7 mM, Ki for 2-keto-4-hydroxyglutarate cleavage: 2.4 mM
2-Ketoglutarate
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competitive, Ki for 2-keto-4-hydroxybutyrate cleavage: 18 mM, Ki for 2-keto-4-hydroxyglutarate cleavage: 18 mM
NaBH4
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incubation of the enzyme with either pyruvate or glyoxylate in the presence of NaBH4 causes extensive loss of aldolase activity concomitant with stable binding of about 1.0-1.5 mol of substrate/mol of enzyme
additional information
-
not inhibitory: mercaptoethanol, EDTA, 1,10-phenanthroline, alpha,alpha'-dipyridyl, or 8-hydroxyquinoline up to 10 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
4-hydroxy-2-oxoglutarate aldolase deficiency
Novel findings in patients with primary hyperoxaluria type III and implications for advanced molecular testing strategies.
4-hydroxy-2-oxoglutarate aldolase deficiency
Primary hyperoxaluria type III-a model for studying perturbations in glyoxylate metabolism.
Hyperoxaluria
Mutations in HOGA1 do Not Confer a Dominant Phenotype Manifesting as Kidney Stone Disease.
Hyperoxaluria
Novel findings in patients with primary hyperoxaluria type III and implications for advanced molecular testing strategies.
Hyperoxaluria, Primary
4-Hydroxy-2-oxoglutarate aldolase inactivity in primary hyperoxaluria type 3 and glyoxylate reductase inhibition.
Hyperoxaluria, Primary
Cellular degradation of 4-hydroxy-2-oxoglutarate aldolase leads to absolute deficiency in primary hyperoxaluria type 3.
Hyperoxaluria, Primary
Clinical characterization of primary hyperoxaluria type 3 in comparison to types 1 and 2: a retrospective cohort study.
Hyperoxaluria, Primary
Dihydrodipicolinate Synthase: Structure, Dynamics, Function, and Evolution.
Hyperoxaluria, Primary
HOGA1 Gene Mutations of Primary Hyperoxaluria Type 3 in Tunisian Patients.
Hyperoxaluria, Primary
Hydroxyproline metabolism in a mouse model of Primary Hyperoxaluria Type 3.
Hyperoxaluria, Primary
Mutation Hot Spot Region in the HOGA1 Gene Associated with Primary Hyperoxaluria Type 3 in the Chinese Population.
Hyperoxaluria, Primary
Mutations in DHDPSL are responsible for primary hyperoxaluria type III.
Hyperoxaluria, Primary
Mutations in HOGA1 do Not Confer a Dominant Phenotype Manifesting as Kidney Stone Disease.
Hyperoxaluria, Primary
Nine novel HOGA1 gene mutations identified in primary hyperoxaluria type 3 and distinct clinical and biochemical characteristics in Chinese children.
Hyperoxaluria, Primary
Novel findings in patients with primary hyperoxaluria type III and implications for advanced molecular testing strategies.
Hyperoxaluria, Primary
Performance evaluation of Sanger sequencing for the diagnosis of primary hyperoxaluria and comparison with targeted next generation sequencing.
Hyperoxaluria, Primary
Possible ethnic associations in primary hyperoxaluria type-III-associated HOGA1 sequence variants.
Hyperoxaluria, Primary
Primary hyperoxaluria type III gene HOGA1 (formerly DHDPSL) as a possible risk factor for idiopathic calcium oxalate urolithiasis.
Hyperoxaluria, Primary
Primary hyperoxaluria type III-a model for studying perturbations in glyoxylate metabolism.
Hyperoxaluria, Primary
Re: Mutations in DHDPSL are Responsible for Primary Hyperoxaluria Type III.
Hyperoxaluria, Primary
Re: primary hyperoxaluria type III gene HOGA1 (formerly DHDPSL) as a possible risk factor for idiopathic calcium oxalate urolithiasis.
Hyperoxaluria, Primary
Regulation of human 4-hydroxy-2-oxoglutarate aldolase by pyruvate and ?-ketoglutarate: implications for primary hyperoxaluria type-3.
Hyperoxaluria, Primary
Renal function can be impaired in children with primary hyperoxaluria type 3.
Hyperoxaluria, Primary
Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria.
Hyperoxaluria, Primary
The enzyme 4-hydroxy-2-oxoglutarate aldolase is deficient in primary hyperoxaluria type 3.
Hyperoxaluria, Primary
The enzyme 4-hydroxy-2-oxoglutarate aldolase is deficient in primary hyperoxaluria type III.
Hyperoxaluria, Primary
Two Novel HOGA1 Splicing Mutations Identified in a Chinese Patient with Primary Hyperoxaluria Type 3.
Hyperoxaluria, Primary
[Genetic aspects of primary hyperoxaluria: epidemiology, ethiology, pathogenesis, and clinical signs of the disorder].
Kidney Calculi
Mutations in HOGA1 do Not Confer a Dominant Phenotype Manifesting as Kidney Stone Disease.
Urolithiasis
Primary hyperoxaluria type III gene HOGA1 (formerly DHDPSL) as a possible risk factor for idiopathic calcium oxalate urolithiasis.
Urolithiasis
Re: primary hyperoxaluria type III gene HOGA1 (formerly DHDPSL) as a possible risk factor for idiopathic calcium oxalate urolithiasis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.23
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE