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Information on EC 4.1.3.16 - 4-Hydroxy-2-oxoglutarate aldolase
for references in articles please use BRENDA:EC4.1.3.16
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EC Tree 4 Lyases
4.1 Carbon-carbon lyases
4.1.3 Oxo-acid-lyases
4.1.3.16 4-Hydroxy-2-oxoglutarate aldolase
IUBMB 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.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 4.1.3.16
- hyperoxalurias
- oxalate
-
stone
- ph2
- grhpr
- hydroxyproline
- urolithiasis
- 2-keto-3-deoxy-6-phosphogluconate
-
nephrocalcinosis
-
alanine-glyoxylate
-
nephrolithiasis
- synthesis
- medicine
showSynonyms
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, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-keto-4-hydroxybutyrate aldolase
-
-
-
-
2-keto-4-hydroxyglutarate aldolase
-
-
-
-
2-keto-4-hydroxyglutaric aldolase
-
-
-
-
2-oxo-4-hydroxyglutarate aldolase
-
-
-
-
2-oxo-4-hydroxyglutaric aldolase
-
-
-
-
4-hydroxy-2-ketoglutarate aldolase
-
-
-
-
4-hydroxy-2-ketoglutaric aldolase
-
-
-
-
aldolase, 4-hydroxy-2-oxoglutarate
-
-
-
-
DL-4-Hydroxy-2-ketoglutarate aldolase
-
-
-
-
EC 4.1.2.1
-
-
formerly
-
EC 4.1.2.31
-
-
formerly
-
hOGA
HOGA1
hydroxyketoglutarate aldolase
-
-
-
-
Hydroxyketoglutaric aldolase
-
-
-
-
KHG-aldolase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
-
-
-
-
elimination
-
-
of an oxo-acid, C-C bond cleavage
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
trans-4-hydroxy-L-proline degradation I
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-Keto-4-hydroxybutyrate
Pyruvate + formaldehyde
-
Substrates: D-isomer favoured
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?
Pyruvate + formaldehyde
2-Keto-4-hydroxybutyrate
-
Substrates: Keq: 4.1 mM
Products: -
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?
4-hydroxy-2-oxoglutarate
?
-
Substrates: catabolism of hydroxyproline, condensation physiologically less important
Products: -
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?
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
-
Substrates: both stereoisomers
Products: -
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?
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
Substrates: -
Products: -
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r
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
Substrates: -
Products: -
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r
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
Substrates: -
Products: -
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?
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
Substrates: -
Products: -
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?
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
-
Substrates: both stereoisomers
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?
D-4-hydroxy-2-oxoglutarate
pyruvate + glyoxylate
-
Substrates: -
Products: -
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?
Glyoxylate + pyruvate
4-Hydroxy-2-ketoglutarate
-
Substrates: higher specificity for pyruvate than for glyoxylate
Products: -
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?
Glyoxylate + pyruvate
4-Hydroxy-2-ketoglutarate
-
Substrates: specific, codensation favoured, Keq: 0.73 mM
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?
Glyoxylate + pyruvate
4-Hydroxy-2-ketoglutarate
-
Substrates: 3-substituted analogs
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?
L-4-hydroxy-2-oxoglutarate
pyruvate + glyoxylate
-
Substrates: -
Products: -
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?
Oxaloacetate
CO2 + pyruvate
-
Substrates: beta-decarboxylation, about 50% as effective as aldolase
Products: -
Products: -
?
additional information
?
-
-
Substrates: functional role of SH-groups, conformational changes during catalysis
Products: -
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?
additional information
?
-
-
Substrates: 2-keto-4-hydroxy-4-methylglutarate, 2-keto-3-deoxy-6-phosphoclucanate cleaved at slow rate
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?
additional information
?
-
-
Substrates: 2-keto-3-deoxyglucarate and 2-keto-4,5-dihydroxyvalerate cleaved at slow rate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
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?
additional information
?
-
Substrates: enzyme performs a retro-aldol cleavage reaction reminiscent of the trimeric 2-keto-3-deoxy-6-phosphogluconate aldolases
Products: -
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?
additional information
?
-
-
Substrates: enzyme performs a retro-aldol cleavage reaction reminiscent of the trimeric 2-keto-3-deoxy-6-phosphogluconate aldolases
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme also has oxaloacetate decarboxylase activity
Products: -
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-
additional information
?
-
-
Substrates: specific for glyoxylate and pyruvate
Products: -
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?
additional information
?
-
-
Substrates: equilibrium favours condensation, Keq: 0.73 1/mM
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?
additional information
?
-
-
Substrates: acts on both stereoisomers
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?
additional information
?
-
-
Substrates: 2-keto-3-deoxyglucarate and 2-keto-4,5-dihydroxyvalerate cleaved at slow rate
Products: -
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-hydroxy-2-oxoglutarate
?
-
Substrates: catabolism of hydroxyproline, condensation physiologically less important
Products: -
Products: -
?
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
Substrates: -
Products: -
Products: -
r
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
Substrates: -
Products: -
Products: -
?
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
Substrates: -
Products: -
Products: -
?
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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-
-
irreversible, in presence of aldehydes, reversible in abscence of aldehydes, 2-keto-4-hydroxyglutarate cleavage, Ki: 0.57 mM
glycolaldehyde
-
competitive, Ki for 2-keto-4-hydroxybutyrate cleavage: 2.7 mM, Ki for 2-keto-4-hydroxyglutarate cleavage: 2.4 mM
2-Ketoglutarate
-
competitive, Ki for 2-keto-4-hydroxybutyrate cleavage: 18 mM, Ki for 2-keto-4-hydroxyglutarate cleavage: 18 mM
NaBH4
-
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
pyruvate
competitive inhibitor, inhibits HOGA1 activity during gluconeogenesis
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
0.056
4-hydroxy-2-oxoglutarate
pH and temperature not specified in the publication, wild-type enzyme
0.139
4-hydroxy-2-oxoglutarate
pH and temperature not specified in the publication, mutant enzyme S198A
0.152
4-hydroxy-2-oxoglutarate
pH and temperature not specified in the publication, mutant enzyme N78T
0.156
4-hydroxy-2-oxoglutarate
pH and temperature not specified in the publication, mutant enzyme S77A
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.31
4-hydroxy-2-oxoglutarate
pH and temperature not specified in the publication, mutant enzyme S77A
0.46
4-hydroxy-2-oxoglutarate
pH and temperature not specified in the publication, mutant enzyme S198A
1.01
4-hydroxy-2-oxoglutarate
pH and temperature not specified in the publication, wild-type enzyme
1.97
4-hydroxy-2-oxoglutarate
pH and temperature not specified in the publication, mutant enzyme N78T
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2
4-hydroxy-2-oxoglutarate
pH and temperature not specified in the publication, mutant enzyme S77A
3.3
4-hydroxy-2-oxoglutarate
pH and temperature not specified in the publication, mutant enzyme S198A
12.2
4-hydroxy-2-oxoglutarate
pH and temperature not specified in the publication, mutant enzyme N78T
19
4-hydroxy-2-oxoglutarate
pH and temperature not specified in the publication, wild-type enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.9
2-oxoglutarate
pH and temperature not specified in the publication, mutant enzyme N78T
22
2-oxoglutarate
pH and temperature not specified in the publication, wild-type enzyme
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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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
the enzyme plays a gatekeeper role in hydroxyproline metabolism
malfunction
-
primary hyperoxaluria type 3 is due to mutations in the 4-hydroxy-2-oxoglutarate aldolase gene
malfunction
enzyme mutations ultimately lead to oxalate accumulation and stone formation in primary hyperoxaluria type 3
malfunction
loss of function in humans causes primary hyperoxaluria type 3 (PH3), a condition characterised by excessive production of oxalate. Loss of HOGA1 function could increase oxalate production in PH3 by decreasing pyruvate availability and metabolic flux through the Krebs cycle
Show AA Sequence and Transmembrane Helices (1063 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
35249
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
4 * 32465, electrospray ionization-Fourier transform mass spectrometry, the enzyme exists exclusively as a tetrameric species in solution
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hamging drop vapor diffusion method, using 100 mM HEPES-NaOH pH 7.0, 200 mM Na2SO4, 22.5% (w/v) PEG 3350, and 20% (v/v) glycerol or 100 mM Tris-HCl pH 8.0 and 1.8 M ammonium sulfate
to 1.97 A resolution, crystal structure of enzyme bound to pyruvate. Modeling of the 4-hydroxy-2-oxoglutarate-Schiff base intermediate and kinetic analyses of site-directed mutants support the importance of Lys196 as the nucleophile, Tyr168 and Ser77 as components of a proton relay, and Asn78 and Ser198 as unique residues that facilitate substrate binding
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C257G
natural mutation associated with Primary Hyperoxaluria type 3. Mutant is quite unstable, has a tendency to aggregate, and retains no measurable activity
DeltaE315
natural mutation associated with Primary Hyperoxaluria type 3. Mutant is quite unstable, has a tendency to aggregate, and retains no measurable activity
G287V
K196A
N78T
P190L
R255X
a truncation of 71 residues from the C-terminus associated with Primary Hyperoxaluria type 3. Mutant is quite unstable, has a tendency to aggregate, and retains no measurable activity
R303C
natural mutation associated with Primary Hyperoxaluria type 3. Mutant is quite unstable, has a tendency to aggregate, and retains no measurable activity
R70P
natural mutation associated with Primary Hyperoxaluria type 3. Mutant is quite unstable, has a tendency to aggregate, and retains no measurable activity
R97C
natural mutation associated with Primary Hyperoxaluria type 3. Mutant is quite unstable, has a tendency to aggregate, and retains no measurable activity
S198A
S77A
T280I
natural mutation associated with Primary Hyperoxaluria type 3. Mutant is quite unstable, has a tendency to aggregate, and retains no measurable activity
Y168F
Y39X/R70X
naturally occuring mutations in a patient with type 3 atypical primary hyperoxaluria
G287V
natural mutation associated with Primary Hyperoxaluria type 3. Mutant is quite unstable, has a tendency to aggregate, and retains no measurable activity
N78T
no effect on oxaloacetate decarboxylase kinetics relative to wild-type enzyme but the KM for the aldolase substrate increases 3fold and kcat by 2fold resulting in no overall significant difference in efficiency. 2-oxoglutarate is a more potent inhibitor of the N78T mutant aldolase activity as compared to wild-type enzyme. kcat/Km for 4-hydroxy-2-oxoglutarate is 64% of the wild-type value
P190L
natural mutation associated with Primary Hyperoxaluria type 3. Mutant is quite unstable, has a tendency to aggregate, and retains no measurable activity
S198A
the KM for the aldolase substrate is increased 3fold, the kcat is reduced by 2fold. kcat/Km for 4-hydroxy-2-oxoglutarate is 17% of the wild-type value
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
irreversibly inactivated by aminonitrile formation from cyanide and enzyme-substrate complex
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4¦C, Tris-HCl buffer, pH 7.4, 40% saturated with ammonium sulfate, 6 months, kidney enzyme
-
4°C, 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
-
4°C, 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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
phenyl Sepharose column chromatography, Sepharose Q column chromatography, and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
genotyping in 28 patients with type 3 atypical primary hyperoxaluria, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
mutations in the gene encoding for 4-hydroxy-2-oxoglutarate aldolase are associated with an excessive production of oxalate in Primary Hyperoxaluria type 3, PH3. Analysis of nine PH3 human variants reveals that all nine PH3 variants are quite unstable, have a tendency to aggregate, and retain no measurable activity. A buildup of 4-hydroxy-2-oxoglutarate takes place in the urine, sera and liver samples from PH3 patients. One hypothetical component of the molecular basis for the excessive oxalate production in PH3 appears to be the inhibition of glyoxylate reductase by 4-hydroxy-2-oxoglutarate, resulting in a phenotype similar to Primary Hyperoxaluria type 2
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Adams, E.
Enzymes and intermediates of hydroxyproline degradation
Methods Enzymol.
17B
266-306
1971
Rattus norvegicus
-
brenda
Kuratomi, K.; Fukunaga, K.
The metabolism of gamma-hydroxyglutamate in rat liver. 1. Enzymic synthesis of gamma-hydroxy-alpha-ketoglutarate from pyruvate and glyoxylate
Biochim. Biophys. Acta
78
617-628
1963
Rattus norvegicus
brenda
Lane, R.S.; Shapley, A.; Dekker, E.E.
2-keto-4-Hydroxybutyrate aldolase. Identification as 2-keto-4-hydroxyglutarate aldolase, catalytic properties, and role in mammalian metabolism of L-homoserine
Biochemistry
10
1353-1364
1971
Bos taurus, Mammalia
brenda
Kobes, R.D.; Dekker, E.E.
Variant properties of bovine liver 2-keto-4-hydroxyglutarate aldolase: its beta-decarboxylase activity, lack of substrate stereospecificity, and structural requirements for binding substrate analogs
Biochim. Biophys. Acta
251
238-250
1971
Bos taurus
brenda
Dekker, E.E.; Kobes, R.D.; Grady, S.R.
2-keto-4-Hydroxyglutarate aldolase from bovine liver
Methods Enzymol.
42C
280-285
1975
Bos taurus
brenda
Hansen, B.A.; Dekker, E.E.
Inactivation of bovine liver 2-keto-4-hydroxyglutarate aldolase by cyanide in the presence of aldehydes
Biochemistry
15
2912-2917
1976
Bos taurus
brenda
Lane, R.S.; Hansen, B.A.; Dekker, E.E.
Sulfhydryl groups in relation to the structure and catalytic properties of 2-oxo-4-hydroxyglutarate aldolase from bovine liver
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Homo sapiens (Q86XE5), Homo sapiens
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Use of a novel microtitration protocol to obtain diffraction-quality crystals of 4-hydroxy-2-oxoglutarate aldolase from Bos taurus
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Regulation of human 4-hydroxy-2-oxoglutarate aldolase by pyruvate and alpha-ketoglutarate Implications for primary hyperoxaluria type-3
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Homo sapiens (Q86XE5)
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