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. 1967 Aug;104(2):557–564. doi: 10.1042/bj1040557

The formation of ornithine from proline in animal tissues

A D Smith 1,*, M Benziman 1, H J Strecker 1
PMCID: PMC1270620  PMID: 6048797

Abstract

1. Homogenates of liver or kidney from rat, mouse, dog and guinea pig formed ornithine from proline but not from glutamate. Rat kidney was most active in this reaction and was used for further studies. 2. The overall reaction was found to be catalysed by proline oxidase to yield glutamic γ-semialdehyde, followed by transamination of this product with glutamate as catalysed by ornithine–keto acid aminotransferase. 3. The unfavourable equilibrium of the ornithine–keto acid aminotransferase reaction was overcome chiefly by glutamate dehydrogenase in the tissue, which removed the α-oxoglutarate produced, by reduction with endogenous ammonia and NADH. 4. Aspartate aminotransferase in these preparations also aided in the removal of α-oxoglutarate. In this case the overall reaction was driven also by the rapid decarboxylation of oxaloacetate. 5. No evidence could be found for a pathway of ornithine synthesis involving acylated intermediates as has been observed in some micro-organisms. 6. The rate of ornithine synthesis in homogenates of several rat tissues paralleled the activity of ornithine–keto acid aminotransferase in these tissues, indicating that this enzyme was rate-determining for the synthesis. 7. The possible influence of these reactions on urea synthesis is discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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