Glyoxylate metabolism by isolated rat liver peroxisomes

Isolated rat liver peroxisomes catalyze the reduction of glyoxylate to glycolate. The peroxisomal glyoxylate reductase preferentially utilizes NADH and glyoxylate. It also reduces hydroxypyruvate and pyruvate, but no dehydrogenase activity is measurable at pH 9.2. Michaelis constants were 11.5 mM fo...

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Published inBiochimica et biophysica acta Vol. 215; no. 3; pp. 449 - 455
Main Authors Vandor, S.L., Tolbert, N.E.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 22.09.1970
Subjects
Alcohol Oxidoreductases - metabolism
Animals
Carbon Isotopes
Centrifugation, Density Gradient
Electron Transport
Female
Glycolates - biosynthesis
Glyoxylates - metabolism
Hydrogen-Ion Concentration
Kinetics
Liver - cytology
Liver - metabolism
NAD - metabolism
Pyruvates - metabolism
Rats
Transaminases - metabolism
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Summary:Isolated rat liver peroxisomes catalyze the reduction of glyoxylate to glycolate. The peroxisomal glyoxylate reductase preferentially utilizes NADH and glyoxylate. It also reduces hydroxypyruvate and pyruvate, but no dehydrogenase activity is measurable at pH 9.2. Michaelis constants were 11.5 mM for glyoxylate and 10.5 μM for NADH, and the pH optimum was 6.4. A glutamate-glyoxylate aminotransferase (EC 2.6.1.4) is also present in rat liver peroxisomes. NADH-glyoxylate reductase (EC 1.1.1.26) in liver peroxisomes may function in a substrate-mediated electron shuttle for the oxidation of cellular NADH.
Bibliography:ObjectType-Article-1
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ISSN:0304-4165
0006-3002
1872-8006
DOI:10.1016/0304-4165(70)90095-4