Regulatory effects of fatty acyl-coenzyme A derivatives on phosphate-activated pig brain and kidney glutaminase in vitro.

The Biochemical Journal
E Kvamme, I A Torgner

Abstract

1. Fatty n-acyl-CoA derivatives in the concentration range 5muM-0.1mM and with 5-18 fatty acyl carbons have dual effects on phosphate-activated glutaminase from pig brain and kidney. Generally, fatty acyl-CoA derivatives in low concentrations activate the enzyme, but inhibit at higher concentrations; phosphate and citrate potentiate the activation, displaying positive co-operatively, and protect against inactivation. The fatty acyl-CoA derivatives affect glutaminase similarly to Bromothymol Blue, but differently from acetyl-CoA, which activates the enzyme only at very low phosphate or citrate concentrations. 2. Saturated fatty acyl-CoA derivatives, with 5-10 fatty acyl carbons, only activate the enzyme in the concentration range 0-0.1 mM. When the fatty acyl chain is elongated, the fatty acyl-CoA derivatives gradually become more powerful inhibitors of glutaminase at the expense of their activating capacity. In particular, palmitoyl-CoA and stearoyl-CoA are strong inhibitors at concentrations (10 muM) at which the corresponding free fatty acids and fatty acyl-carnitine derivatives have no effect. 3. The unsaturated fatty acyl-CoA derivatives, oleoyl-CoA and linoleoyl-CoA, behave as potent activators in the lower part of the con...Continue Reading

Citations

May 1, 1984·Acta Neurologica Scandinavica
Jan 1, 1983·Neurochemical Research·E KvammeI A Torgner
Apr 1, 1989·Neurochemical Research·H AkiyamaT Kaneko
Dec 18, 2001·Journal of Neuroscience Research·E KvammeB Roberg
Apr 1, 1989·Neurochemical Research·H R ZielkeM E Landry
Jul 1, 1985·Irish Journal of Medical Science·D J O'Donovan
Aug 28, 2018·Journal of Medicinal Chemistry·Xi XuJinlei Bian

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