Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.
Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.
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DOI：
10.1021/acs.biochem.8b00123
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发表时间：
2018-06-05
期刊：
影响因子：
2.9
通讯作者：
Davidson VL
中科院分区：
文献类型：
--
作者：
Davidson VL
蛋白质衍生的辅因子是蛋白质中通过一个或多个氨基酸残基的翻译后修饰形成的催化或氧化还原活性位点。这些翻译后修饰是不可逆的，并赋予修饰的氨基酸残基新的功能特性。本展望着重于近年来在这一领域取得的下列进展。色氨酸蒽醌（TTQ）辅因子的生物合成由二血红素酶MauG催化。一个双FeIV氧化还原态的血红素进行三个两电子氧化的特定色氨酸残基通过远程电子转移。与此相反，黄素酶催化的半胱氨酸醌（CTQ）辅因子的生物合成存在于一个新发现的家族的CTQ依赖性氧化酶。在脱羧酶和还原酶类中发现的另一种羰基辅因子，即异戊酰辅因子，是在裂解产物N-末端的前体蛋白的明显自催化裂解过程中形成的。已经表明，至少在某些情况下，与辅助蛋白的结合有助于切割。酪氨酰醌辅因子、托蒽醌（TPQ）和赖氨酸酪氨酰醌（LTQ）分别存在于含铜胺氧化酶和赖氨酰氧化酶中。这些酶的不同家族在人类中的生理作用已被更清楚地定义，并显示出对人类健康具有重大意义。共价交联的氨基酸侧链影响蛋白质中氧化还原活性金属中心的反应性的作用也一直在持续表征。这些包括半乳糖氧化酶和半胱氨酸双加氧酶中的Cys-Tyr种类，以及过氧化氢酶-过氧化物酶KatG中的Met-Tyr-Trp种类。
A protein-derived cofactor is a catalytic or redox-active site in a protein that is formed by post-translational modification of one or more amino acid residues. These post-translational modifications are irreversible and endow the modified amino acid residues with new functional properties. This Perspective focusses on the following advances in this area that have occurred during recent years. The biosynthesis of the tryptophan tryptophylquinone (TTQ) cofactor is catalyzed by a di-heme enzyme, MauG. A bis-FeIV redox state of the hemes performs three two-electron oxidations of specific Trp residues via long-range electron transfer. In contrast, a flavoenzyme catalyzes the biosynthesis of the cysteine tryptophylquinone (CTQ) cofactor present in a newly discovered family of CTQ-dependent oxidases. Another carbonyl cofactor, the pyruvoyl cofactor found in classes of decarboxylases and reductases, is formed during an apparently autocatalytic cleavage of a precursor protein at the N-terminus of the cleavage product. It has been show that in at least some cases, the cleavage is facilitated by binding to an accessory protein. Tyrosylquinonine cofactors, topaquinone (TPQ) and lysine tyrosylquinone (LTQ) are found in copper-containing amine oxidases and lysyl oxidases, respectively. The physiological roles of different families of these enzymes in humans has been more clearly defined and shown to have significant implications towards human health. There has also been continued characterization of the roles of covalently cross-linked amino acid side-chains that influence the reactivity of redox-active metal centers in proteins. These include Cys-Tyr species in galactose oxidase and cysteine dioxygenase, and the Met-Tyr-Trp species in the catalase-peroxidase KatG.
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影响因子：
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