EC Number   |
General Information |
Reference |
|---|
    1.1.1.79 | evolution |
role in the substrate binding mode and role of Leu53 and Trp138 in substrate trafficking is conserved between human and archeal enzymes, modelling, overview |
-, 739674 |
| 1.1.1.79 | evolution |
the deduced amino acid sequence of the enzyme from Paecilomyes thermophila has low similarities to the reported glyoxylate reductases |
-, 740392 |
| 1.1.1.79 | evolution |
the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family |
737745 |
| 1.1.1.79 | evolution |
the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs |
737745 |
| 1.1.1.79 | evolution |
the enzyme belongs to the group of enzymes with the most common NAD(P)-binding fold, the Rossmann fold, as well as other, less common cofactor binding folds (TIM barrel and dihydroquinoate synthase-like folds) |
739782 |
| 1.1.1.79 | evolution |
the primary sequence of cytosolic AtGLYR1 reveals several sequence elements that are consistent with the beta-HAD (beta-hydroxyacid dehydrogenase) protein family, sequence alignment of AtGLYR1 and beta-HAD family members, overview. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs |
737745 |
| 1.1.1.79 | evolution |
the primary sequence of plastidial AtGLYR2 reveals several sequence elements that are consistent with the beta-HAD (beta-hydroxyacid dehydrogenase) protein family, sequence alignment of AtGLYR2 and beta-HAD family members, overview. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs |
737745 |
| 1.1.1.79 | malfunction |
enzyme deficiency causes primary hyperoxaluria type 2 |
739241 |
| 1.1.1.79 | malfunction |
enzyme deficiency is the underlying cause of primary hyperoxaluria type 2 (PH2) and leads to increased urinary oxalate levels, formation of kidney stones and renal failure. Upregulation of glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is associated with intestinal epithelial cells apoptosis in TNBS-induced experimental colitis, the phenomenon also occurs in patients with Crohn's disease. Overexpression of GRHPR is accompanied by active caspase-3 and cleaved poly ADP-ribose polymerase (PARP) accumulation. Knockdown of GRHPR inhibits the accumulation of active caspase-3 and cleaved PARP in TNF-alpha treated HT-29 cells |
739242 |
| 1.1.1.79 | metabolism |
glyoxylate reductase is an important enzyme involved in theglyoxylate metabolism in organism |
-, 740392 |
