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Research Article Free access | 10.1172/JCI106110

Familial hyperlysinemia with lysine-ketoglutarate reductase insufficiency

Joseph Dancis, Joel Hutzler, Rody P. Cox, and Norman C. Woody

Department of Pediatrics, New York University School of Medicine, New York 10016

Department of Medicine, New York University School of Medicine, New York 10016

Department of Pediatrics, Tulane Medical School, New Orleans, Louisiana 70112

Find articles by Dancis, J. in: JCI | PubMed | Google Scholar

Department of Pediatrics, New York University School of Medicine, New York 10016

Department of Medicine, New York University School of Medicine, New York 10016

Department of Pediatrics, Tulane Medical School, New Orleans, Louisiana 70112

Find articles by Hutzler, J. in: JCI | PubMed | Google Scholar

Department of Pediatrics, New York University School of Medicine, New York 10016

Department of Medicine, New York University School of Medicine, New York 10016

Department of Pediatrics, Tulane Medical School, New Orleans, Louisiana 70112

Find articles by Cox, R. in: JCI | PubMed | Google Scholar

Department of Pediatrics, New York University School of Medicine, New York 10016

Department of Medicine, New York University School of Medicine, New York 10016

Department of Pediatrics, Tulane Medical School, New Orleans, Louisiana 70112

Find articles by Woody, N. in: JCI | PubMed | Google Scholar

Published August 1, 1969 - More info

Published in Volume 48, Issue 8 on August 1, 1969
J Clin Invest. 1969;48(8):1447–1452. https://doi.org/10.1172/JCI106110.
© 1969 The American Society for Clinical Investigation
Published August 1, 1969 - Version history
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Abstract

Fibroblasts grown in tissue culture from the skin of normal subjects have lysine-ketoglutarate reductase activity (lysine: α-ketoglutarate: triphosphopyridine nucleotide (TPNH) oxidoreductase (ε-N-[L-glutaryl-2]-L-lysine forming)). The activity of the enzyme is considerably reduced in the skin fibroblasts grown from three siblings with hyperlysinemia. The high concentrations of lysine in the blood of these patients, the previous demonstration in the intact subject of a reduction in the ability to degrade lysine, and the present demonstration of diminished lysine-ketoglutarate reductase activity, accurately define the metabolic defect and establish the saccharopine (ε-N-[L-glutaryl-2]-L-lysine) pathway as the major degradative pathway for lysine in the human.

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