glyoxylate + alanine => glycine + pyruvate [peroxisome]
glyoxylate + L-Ala → Gly + PYR
- Reactome
- R-HSA-389684
- Compartment
- peroxisomal matrix
- Rhea
- RHEA:24249
Inputs
- glyoxylateCHEBI:36655, C2HO3, peroxisomal matrix
- L-AlaCHEBI:57972, C3H7NO2, peroxisomal matrix
Outputs
- GlyCHEBI:57305, C2H5NO2, peroxisomal matrix
- PYRCHEBI:15361, C3H3O3, peroxisomal matrix
Catalysed by
- L-alanine:glyoxylate transaminase activity of AGXT dimer [peroxisomal matrix]EC 2.6.1.44
Literature
- Overexpression of human alanine:glyoxylate aminotransferase in Escherichia coli: renaturation from guanidine-HCl and affinity for pyridoxal phosphate co-factor Protein Expr Purif, 2005
- Further studies on the activity and subcellular distribution of alanine:glyoxylate aminotransferase in the livers of patients with primary hyperoxaluria type 1 Clin Sci (Lond), 1988
- Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1 J Cell Biol, 1990
- Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon Biochem J, 1990
- Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1 J Mol Biol, 2003