Hyperoxaluria in L-glyceric aciduria: possible nonenzymic mechanism.

Abstract

Hydroxypyruvate inhibited the oxidation of [1-14C]glyoxylate to [14C] oxalate whether catalyzed by a purified preparation of glycolic acid oxidase from human liver, lactate dehydrogenase, a human liver extract, or a lobe of rat liver. It also brought about the nonenzymic decarboxylation of [1-14C]glyoxylate when it was present in the above assay systems. Radioactive isotope dilution and high-performance liquid chromatography analysis revealed the autooxidation of hydroxypyruvate to oxalate on standing in buffered solution at pH 7.4. In view of these observations, the current hypothesis of the role of lactate dehydrogenase in inducing hyperoxaluria in L-glyceric aciduria has been reexamined, and a possible nonenzymic mechanism by which oxalate may originate from hydroxypyruvate under such conditions has been proposed.

• Authors: K G Raghavan, K E Richardson
• Journal: Biochemical medicine (Biochem Med) Vol. 29 Issue 1 Pg. 114-21 (Feb 1983) ISSN: 0006-2944 [Print] United States
• PMID: 6838496 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Glyceric Acids
• Glyoxylates
• Oxalates
• Pyruvates
• hydroxypyruvic acid

Topics

• Amino Acid Metabolism, Inborn Errors (etiology, metabolism)
• Animals
• Decarboxylation
• Glyceric Acids (urine)
• Glyoxylates (metabolism)
• Humans
• Oxalates (metabolism, urine)
• Pyruvates (metabolism)
• Rats