EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
4.1.3.16 | 5250 |
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 |
7016177 |
4.1.3.16 | 5237 |
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 |
14089442 |
4.1.3.16 | 713711 |
Mutations in DHDPSL are responsible for primary hyperoxaluria type III |
Am. J. Hum. Genet. |
87 |
392-399 |
2010 |
Homo sapiens |
20797690 |
4.1.3.16 | 723542 |
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 |
21998747 |
4.1.3.16 | 728378 |
The enzyme 4-hydroxy-2-oxoglutarate aldolase is deficient in primary hyperoxaluria type 3 |
Nephrol. Dial. Transplant. |
27 |
3191-3195 |
2012 |
Homo sapiens |
22391140 |
4.1.3.16 | 721727 |
4-Hydroxy-2-oxoglutarate aldolase inactivity in primary hyperoxaluria type 3 and glyoxylate reductase inhibition |
Biochim. Biophys. Acta |
1822 |
1544-1552 |
2012 |
Homo sapiens |
22771891 |
4.1.3.16 | 746641 |
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 |
25372828 |
4.1.3.16 | 747772 |
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 |
27096395 |
4.1.3.16 | 748294 |
HOGA1 gene mutations of primary hyperoxaluria type 3 in tunisian patients |
J. Clin. Lab. Anal. |
31 |
e22053 |
2017 |
Homo sapiens |
27561601 |
4.1.3.16 | 746867 |
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 |
30062480 |