Reference on EC 4.1.3.16 - 4-Hydroxy-2-oxoglutarate aldolase
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Adams, E.
Enzymes and intermediates of hydroxyproline degradation
Methods Enzymol.
17B
266-306
1971
Rattus norvegicus
-
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
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
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
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
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
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
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
Scholtz, J.M.; Schuster, S.M.
Substrates of hydroxyketoglutarate aldolase
Bioorg. Chem.
12
229-234
1984
Rattus norvegicus
-
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
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
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
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
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
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
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
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)
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)
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