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首页> 外文期刊>Biochemistry >Acyl-CoA binding proteins inhibit the nonenzymic S-acylation of cysteinyl-containing peptide sequences by long-chain acyl-CoAs.
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Acyl-CoA binding proteins inhibit the nonenzymic S-acylation of cysteinyl-containing peptide sequences by long-chain acyl-CoAs.

机译：酰基辅酶A结合蛋白通过长链酰基辅酶A抑制含半胱氨酰的肽序列的非酶S-酰化作用。

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摘要

Acyl-CoA binding proteins (ACBPs) from rat and bovine liver were found to inhibit the nonenzymic S-acylation of two representative types of peptides by long-chain acyl-CoAs. As demonstrated previously [Quesnel, S. & Silvius, J. R. (1994) Biochemistry 33 13340-13348; Bharadwaj, M., & Bizzozero, O. A. (1995) J. Neurochem. 65, 1805-1815], peptides with the sequences myristoyl-GCG, myristoyl-GCV, and IRYCWLRR-NH2, all representing physiological S-acylation sites in mammalian proteins, become S-acylated at appreciable rates in the presence of long-chain acyl-CoAs and large unilamellar lipid vesicles. Addition of ACBP at physiological molar ratios with respect to long-chain acyl-CoAs strongly inhibits the spontaneous S-acylation reaction, in a manner that can be quantitatively described by assuming that the ACBP sequesters the acyl-CoA with nanomolar affinity in a complex unable to serve as an S-acyl donor. From these results, we calculate that at physiological (intracellular) concentrations of ACBP, long-chain acyl-CoAs, and membrane lipids the expected half-times for spontaneous S-acylation of such protein sequences by long-chain acyl-CoAs will lie in the range of several tens of hours. The nonenzymic reaction of protein cysteine residues with long-chain acyl-CoAs is thus unlikely to contribute significantly to the physiological modification of signaling and other proteins that show relatively rapid rates of S-acylation in mammalian cells. However, it cannot be excluded that a nonenzymic reaction with long-chain acyl-CoAs could contribute to the physiological S-acylation of certain membrane proteins if the latter exhibit very slow kinetics of S-acylation in vivo.
机译：发现来自大鼠和牛肝的酰基辅酶A结合蛋白（ACBP）通过长链酰基辅酶A抑制两种代表性类型的肽的非酶S-酰化作用。如先前所证明的[Quesnel，S。＆Silvius，J.R。（1994）Biochemistry 33 13340-13348; Proc.Natl.Acad.Sci.USA 90：5873-5877。 Bharadwaj，M。和Bizzozero，O.A。（1995）J.Neurochem。 65，1805-1815]，序列myristoyl-GCG，myristoyl-GCV和IRYCWLRR-NH2的肽全都代表哺乳动物蛋白质中的生理S-酰化位点，在长链酰基的存在下以可观的速率被S-酰化-CoAs和大的单层脂质囊泡。相对于长链酰基辅酶A，以生理摩尔比添加ACBP强烈抑制了自发的S-酰化反应，其方式可以通过假设ACBP螯合具有纳摩尔摩尔亲和力的酰基辅酶A来定量地描述。充当S-酰基供体从这些结果，我们计算出，在生理（细胞内）浓度的ACBP，长链酰基辅酶A和膜脂的作用下，长链酰基辅酶A对此类蛋白质序列进行自发S-酰化的预期半衰期将位于几十小时的范围。因此，蛋白质半胱氨酸残基与长链酰基辅酶A的非酶反应不太可能显着促进信号转导和其他蛋白质的生理修饰，这些蛋白质在哺乳动物细胞中显示出相对较快的S-酰化速率。但是，不能排除的是，如果某些膜蛋白在体内表现出非常慢的S-酰化动力学，则与长链酰基辅酶A的非酶促反应可能有助于某些膜蛋白的生理S-酰化。

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