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2-Keto-4-hydroxybutyrate
?
-
metabolism of L-homoserine
-
-
?
2-Keto-4-hydroxybutyrate
Pyruvate + formaldehyde
-
D-isomer favoured
-
?
3-(4-hydroxyphenyl)pyruvate + glyoxylate
?
-
-
-
-
?
3-(4-imidazole)pyruvate + glyoxylate
?
-
-
-
-
?
4-hydroxy-2-oxoglutarate
?
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
acetaldehyde + glyoxylate
?
-
-
-
-
?
D-4-hydroxy-2-oxoglutarate
pyruvate + glyoxylate
Glyoxylate + pyruvate
4-Hydroxy-2-ketoglutarate
L-4-hydroxy-2-oxoglutarate
pyruvate + glyoxylate
Oxaloacetate
CO2 + pyruvate
pyruvaldehyde + glyoxylate
?
-
-
-
-
?
Pyruvate + formaldehyde
2-Keto-4-hydroxybutyrate
-
Keq: 4.1 mM
-
?
pyruvate + glyoxylate
D-4-hydroxy-2-oxoglutarate
-
-
-
-
r
pyruvic acid ethyl ester + glyoxylate
?
-
-
-
-
?
pyruvic acid methyl ester + glyoxylate
?
-
-
-
-
?
additional information
?
-
4-hydroxy-2-oxoglutarate
?
-
catabolism of hydroxyproline, condensation physiologically less important
-
-
?
4-hydroxy-2-oxoglutarate
?
-
-
-
-
?
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
-
-
-
?
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
-
-
-
?
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
-
both stereoisomers
-
?
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
-
-
-
r
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
-
-
-
-
?
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
-
-
-
?
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
-
-
-
r
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
-
-
-
-
r
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
-
-
-
?
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
-
both stereoisomers
-
?
D-4-hydroxy-2-oxoglutarate
pyruvate + glyoxylate
-
-
-
-
r
D-4-hydroxy-2-oxoglutarate
pyruvate + glyoxylate
-
-
-
-
?
Glyoxylate + pyruvate
4-Hydroxy-2-ketoglutarate
-
higher specificity for pyruvate than for glyoxylate
-
-
?
Glyoxylate + pyruvate
4-Hydroxy-2-ketoglutarate
-
specific, codensation favoured, Keq: 0.73 mM
-
?
Glyoxylate + pyruvate
4-Hydroxy-2-ketoglutarate
-
3-substituted analogs
-
-
?
L-4-hydroxy-2-oxoglutarate
pyruvate + glyoxylate
-
-
-
-
?
L-4-hydroxy-2-oxoglutarate
pyruvate + glyoxylate
-
-
-
-
r
L-4-hydroxy-2-oxoglutarate
pyruvate + glyoxylate
-
-
-
-
?
Oxaloacetate
CO2 + pyruvate
-
-
-
?
Oxaloacetate
CO2 + pyruvate
-
-
-
-
?
Oxaloacetate
CO2 + pyruvate
-
beta-decarboxylation, about 50% as effective as aldolase
-
?
Oxaloacetate
CO2 + pyruvate
-
-
-
-
?
additional information
?
-
-
mechanism
-
-
?
additional information
?
-
-
mechanism
-
-
?
additional information
?
-
-
mechanism
-
-
?
additional information
?
-
-
functional role of SH-groups, conformational changes during catalysis
-
-
?
additional information
?
-
-
Keq: 11 mM
-
-
?
additional information
?
-
-
2-keto-4-hydroxy-4-methylglutarate, 2-keto-3-deoxy-6-phosphoclucanate cleaved at slow rate
-
-
?
additional information
?
-
-
acts on both stereoisomers
-
-
?
additional information
?
-
-
2-keto-3-deoxyglucarate and 2-keto-4,5-dihydroxyvalerate cleaved at slow rate
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
enzyme performs a retro-aldol cleavage reaction reminiscent of the trimeric 2-keto-3-deoxy-6-phosphogluconate aldolases
-
-
?
additional information
?
-
-
enzyme performs a retro-aldol cleavage reaction reminiscent of the trimeric 2-keto-3-deoxy-6-phosphogluconate aldolases
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
specific for glyoxylate and pyruvate
-
-
?
additional information
?
-
-
equilibrium favours condensation, Keq: 0.73 1/mM
-
-
?
additional information
?
-
-
acts on both stereoisomers
-
-
?
additional information
?
-
-
2-keto-3-deoxyglucarate and 2-keto-4,5-dihydroxyvalerate cleaved at slow rate
-
-
?
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2-Ketobutyrate
-
competitive, Ki for 2-keto-4-hydroxybutyrate cleavage: 53 mM, Ki for 2-keto-4-hydroxyglutarate cleavage: 52 mM
4-hydroxy-2-oxoglutarate
-
substrate inhibition, Ki: 35 mM
5,5'-dithiobis(2-nitrobenzoate)
-
glyoxylate and pyruvate protect
Bromopyruvate
-
Ki: 0.018 mM
chloride
-
41% inhibition at 40 mM
CN-
-
irreversible, in presence of aldehydes, reversible in abscence of aldehydes, 2-keto-4-hydroxyglutarate cleavage, Ki: 0.57 mM
Cu2+
-
93% inhibition at 2 mM
cysteine
-
65% inhibition at 10 mM
dithiodipyridine
-
kidney enzyme
glycolaldehyde
-
competitive, Ki for 2-keto-4-hydroxybutyrate cleavage: 2.7 mM, Ki for 2-keto-4-hydroxyglutarate cleavage: 2.4 mM
Glyoxal
-
36% inhibition at 20 mM
Hydroxypyruvate
-
91% inhibition at 20 mM
iodoacetate
-
10% inhibition at 10 mM
Mn2+
-
65% inhibition at 10 mM; kidney enzyme, 65% inhibition at 10 mM
N-ethylmaleimide
-
64% inhibition at 10 mM
oxaloacetate
-
competitive, Ki: 0.22 mM
p-mercuribenzoate
-
kidney enzyme
sulfhydryl-reacting reagents
-
-
-
2-Ketoglutarate
-
competitive, Ki for 2-keto-4-hydroxybutyrate cleavage: 18 mM, Ki for 2-keto-4-hydroxyglutarate cleavage: 18 mM
2-Ketoglutarate
-
12% inhibition at 20 mM
glyoxylate
-
bovine enzyme inhibited at lower concentrations than E. coli enzyme
Hg2+
-
100% inhibition at 1 microM; kidney enzyme, complete inhibition at 1 mM
Hg2+
-
complete inhibition at 2 mM
NaBH4
-
-
NaBH4
-
azomethine formation with substrates and substrate analogues
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
NaBr
-
-
NaBr
-
18% inhibition at 50 mM, only condensation
NaF
-
-
NaF
-
15% inhibition at 50 mM, only condensation
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
complete inhibition at 10 mM
pyruvate
-
-
additional information
-
-
-
additional information
-
not inhibitory: mercaptoethanol, EDTA, 1,10-phenanthroline, alpha,alpha'-dipyridyl, or 8-hydroxyquinoline up to 10 mM
-
additional information
-
double inhibitor studies
-
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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
Folding Defects Leading to Primary Hyperoxaluria.
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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0.14
(D)-4-hydroxy-alpha-ketoglutarate
-
-
3.1
2-Keto-4-hydroxybutyrate
-
-
7.7
3-(4-hydroxyphenyl)pyruvate
-
-
7.4
3-(4-imidazole)pyruvate
-
-
0.008 - 0.281
4-hydroxy-2-oxoglutarate
0.1 - 1.33
4-hydroxy-alpha-ketoglutarate
0.031 - 0.11
D-4-hydroxy-2-oxoglutarate
0.024 - 71
L-4-hydroxy-2-oxoglutarate
30
oxaloacetate
-
condensation with glyoxylate
2.8
Pyruvic acid ethyl ester
-
-
3.2
pyruvic acid methyl ester
-
-
additional information
additional information
-
0.008
4-hydroxy-2-oxoglutarate
mutant Y140F, pH 8.5, 37°C
0.011
4-hydroxy-2-oxoglutarate
wild-type, pH 8.5, 37°C
0.016
4-hydroxy-2-oxoglutarate
mutant N78T, pH 8.5, 37°C
0.044
4-hydroxy-2-oxoglutarate
mutant S198A, pH 8.5, 37°C
0.058
4-hydroxy-2-oxoglutarate
mutant S77T, pH 8.5, 37°C
0.066
4-hydroxy-2-oxoglutarate
mutant N78A, pH 8.5, 37°C
0.077
4-hydroxy-2-oxoglutarate
mutant S198T, pH 8.5, 37°C
0.082
4-hydroxy-2-oxoglutarate
mutant S77V, pH 8.5, 37°C
0.084
4-hydroxy-2-oxoglutarate
mutant S77A, pH 8.5, 37°C
0.281
4-hydroxy-2-oxoglutarate
mutant N78Q, pH 8.5, 37°C
0.1
4-hydroxy-alpha-ketoglutarate
-
-
1.33
4-hydroxy-alpha-ketoglutarate
-
-
0.031
D-4-hydroxy-2-oxoglutarate
-
pH 8.3, 37°C
0.11
D-4-hydroxy-2-oxoglutarate
-
-
0.024
L-4-hydroxy-2-oxoglutarate
-
pH 8.3, 37°C
0.22
L-4-hydroxy-2-oxoglutarate
-
-
71
L-4-hydroxy-2-oxoglutarate
-
-
10
pyruvate
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
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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
K196A
complete loss of activity
N78A
20% of wild-type activity
N78Q
4% of wild-type activity
N78T
45% of wild-type activity
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
9% of wild-type activity
S198T
18% of wild-type activity
S77A
5% of wild-type activity
S77T
2% of wild-type activity
S77V
2% of wild-type activity
T280I
natural mutation associated with Primary Hyperoxaluria type 3. Mutant is quite unstable, has a tendency to aggregate, and retains no measurable activity
Y140F
122% of wild-type activity
Y168F
complete loss of activity
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
G287V
-
the mutation is associated with primary hyperoxaluria type 3
P190L
natural mutation associated with Primary Hyperoxaluria type 3. Mutant is quite unstable, has a tendency to aggregate, and retains no measurable activity
P190L
-
the mutation is associated with primary hyperoxaluria type 3
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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
Biochim. Biophys. Acta
481
212-221
1977
Bos taurus
brenda
Grady, S.R.; Wang, J.K.; Dekker, E.E.
Steady-state kinetics and inhibition studies of the aldol condensation reaction catalized by bovine liver and Escherichia coli 2-keto-4-hydroxyglutarate aldolase
Biochemistry
20
2497-2502
1981
Bos taurus
brenda
Scholtz, J.M.; Schuster, S.M.
Substrates of hydroxyketoglutarate aldolase
Bioorg. Chem.
12
229-234
1984
Rattus norvegicus
-
brenda
Anderson, M.; Scholtz, J.M.; Schuster, S.M.
Rat liver 4-hydroxy-2-ketoglutarate aldolase: purification and kinetic characterization
Arch. Biochem. Biophys.
236
82-97
1985
Rattus norvegicus
brenda
Dekker, E.E.; Kitson, R.P.
2-keto-4-Hydroxyglutarate aldolase: purification of the homogeneous enzyme from bovine kidney
J. Biol. Chem.
267
10507-10514
1992
Bos taurus
brenda
Belostotsky, R.; Seboun, E.; Idelson, G.H.; Milliner, D.S.; Becker-Cohen, R.; Rinat, C.; Monico, C.G.; Feinstein, S.; Ben-Shalom, E.; Magen, D.; Weissman, I.; Charon, C.; Frishberg, Y.
Mutations in DHDPSL are responsible for primary hyperoxaluria type III
Am. J. Hum. Genet.
87
392-399
2010
Homo sapiens (Q86XE5), Homo sapiens
brenda
Riedel, T.J.; Knight, J.; Murray, M.S.; Milliner, D.S.; Holmes, R.P.; Lowther, W.T.
4-Hydroxy-2-oxoglutarate aldolase inactivity in primary hyperoxaluria type 3 and glyoxylate reductase inhibition
Biochim. Biophys. Acta
1822
1544-1552
2012
Homo sapiens (Q86XE5), Homo sapiens
brenda
Riedel, T.J.; Johnson, L.C.; Knight, J.; Hantgan, R.R.; Holmes, R.P.; Lowther, W.T.
Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria
PLoS ONE
6
e26021
2011
Homo sapiens (Q86XE5), Homo sapiens
brenda
Williams, E.L.; Bockenhauer, D.; vant Hoff, W.G.; Johri, N.; Laing, C.; Sinha, M.D.; Unwin, R.; Viljoen, A.; Rumsby, G.
The enzyme 4-hydroxy-2-oxoglutarate aldolase is deficient in primary hyperoxaluria type 3
Nephrol. Dial. Transplant.
27
3191-3195
2012
Homo sapiens (Q86XE5), Homo sapiens
brenda
Huang, A.; Baker, E.; Loomes, K.
Use of a novel microtitration protocol to obtain diffraction-quality crystals of 4-hydroxy-2-oxoglutarate aldolase from Bos taurus
Acta Crystallogr. Sect. F
70
1546-1549
2014
Bos taurus (Q0P5I5), Bos taurus
brenda
Schapfl, M.; Baier, S.; Fries, A.; Ferlaino, S.; Waltzer, S.; Mueller, M.; Sprenger, G.A.
Extended substrate range of thiamine diphosphate-dependent MenD enzyme by coupling of two C-C-bonding reactions
Appl. Microbiol. Biotechnol.
102
8359-8372
2018
Escherichia coli (P0A955)
brenda
MacDonald, J.R.; Huang, A.D.; Loomes, K.M.
Cellular degradation of 4-hydroxy-2-oxoglutarate aldolase leads to absolute deficiency in primary hyperoxaluria type 3
FEBS Lett.
590
1467-1476
2016
Homo sapiens (Q86XE5)
brenda
Mdimegh, S.; Aquaviva-Bourdain, C.; Omezzine, A.; Souche, G.; Mbarek, I.; Abidi, K.; Gargah, T.; Abroug, S.; Bouslama, A.
HOGA1 gene mutations of primary hyperoxaluria type 3 in tunisian patients
J. Clin. Lab. Anal.
31
e22053
2017
Homo sapiens
brenda