It catalyzes the reverse reaction as well, and is therefore essential in creating ornithine from the starting substrate proline.

[2] The structure of the OAT protein has been resolved using X-ray crystallography and shows similarity to other subgroup 2 aminotransferases such as dialkyglucine decarboxylatse.

[3] The OAT protein functions as a dimer and each monomer consists of a large domain, which contributes most to subunit interface, and a C-terminal small domain, and an N-terminal region containing a helix, loop, and three-stranded beta-meander.

[2] In the latter, abnormality of mitochondrial import causes ectopic accumulation of the OAT protein in the cytosol followed by rapid degradation by proteolysis.

[4][5][6][7] The mechanism of gyrate atrophy of choroid and retina is thought to involve the toxicity of glyoxylate.