Peroxisomal alanine:glyoxylate aminotransferase

Hyperoxaluria type 1 is due to functional efficiency of the liver specific peroxisomal enzyme alanine-glyoxylate aminotransferase. It leads to severe renal failure. The nervous system is not affected. 

Located in the peroxisomes of liver, L-alanine-glyoxylate aminotransferase catalyzes the transamination of alanine and glyoxylate to form pyruvate and glycine. A rare inborn error of metabolism manifested as hyperoxaluria is due to a deficiency of this enzyme. 

Leiper JM, Oatey PB, Danpure CJ Inhibition of alanine glyoxylate aminotransferase 1 dimerization is a prerequisite for its peroxisome-to-mitochondrion mistargeting in primary hyperoxaluria type 1. J Cell Biol 1996 135 939-951. 

The enzymes utilizing serine as amino donor and glyoxylate as amino acceptor are considered together here. Much attention has been paid to these aminotransferases, with the role of these enzymes in photorespiration being a particular focus of interest (see Keys, this volume. Chapter 9). Initial studies on impure extracts indicated the presence of glyoxylate aminotransferases which could use glutamate, aspartate, alanine, and serine as amino donors. The best donor to glyoxylate varied from one tissue to another (Cossins and Sinha, 1965). Leaf peroxisomes were subsequently shown to... 

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