UniPlot Summary
//Function Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces
hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate.
//Catalytic activity Glycolate + NADP+ = glyoxylate + NADPH. D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H.
//Subunit structure Homodimer. Ref.1 Ref.7
//Tissue specificity Ubiquitous. Most abundantly expressed in the liver. Ref.5
//Involvement in disease Defects in GRHPR are the cause of hyperoxaluria primary type 2 (HP2) [MIM:260000]; also known as primary
hyperoxaluriatype II (PH2). HP2 is a disorder where the main clinical manifestation is calcium oxalatenephrolithiasis though chronic as well
as terminal renal insufficiency has been described. It is characterized by an elevated urinary excretion of oxalate and L-glycerate. Ref.2
//Sequence similarities Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
Reference
1. "Identification and expression of a cDNA for human hydroxypyruvate/glyoxylatereductase." Rumsby G. et al. Biochim. Biophys. Acta
1446:383-388(1999) [PubMed: 10524214] [Abstract]. Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT. Tissue: Liver.
2. "The gene encoding hydroxypyruvatereductase (GRHPR) is mutated in patients with primary hyperoxaluria type II." Cramer S.D. et al.
Hum. Mol. Genet. 8:2063-2069(1999) [PubMed: 10484776] [Abstract]. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA],
INVOLVEMENT IN HP2. Tissue: Liver.
3. Liu B. et al. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE
MRNA]. Tissue: Aorta
| Product Specifications |
| Application |
ELISA, WB |
| Reactivity |
Human |
| Clonality |
Monoclonal (Clone No.: 7G1) |
| Host |
Mouse |
