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氨基酸氧化酶的鉴定和开发。

Identification and development of amino acid oxidases.

机构信息

Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, mizu, Toyama 939-0398, Japan.

Toyama Institute of Health, 17-1 Nakataikoyama, Imizu, Toyama 939-0363, Japan.

出版信息

Curr Opin Chem Biol. 2019 Apr;49:76-83. doi: 10.1016/j.cbpa.2018.10.020. Epub 2018 Nov 15.

Abstract

Amino acid oxidases are an important class of enzymes that mostly participate in the oxidation of amino acids using FAD as a cofactor. Many of them function in the catabolism of amino acids with wider substrate specificities. On the other hand, based on the recent, successful use of the enzymes for diagnoses with new cofactor and mechanism, highly selective enzymes have been screened from Nature, and many new enzymes have been discovered and further characterized by X-ray crystallography. As a result of the screening for amino acid oxidases with biosynthetic or antibiotic functions, l-Trp oxidase, l-Lys oxidases, and Gly oxidase have been found. The pyridoxal phosphate-dependent l-Arg oxidase has the intriguing new activity of hydroxylating unactivated CC bonds. A new amine oxidase was created by the protein engineering of d-amino acid oxidase. Recent developments in the characterization of amino acid oxidases and their applications are summarized.

摘要

氨基酸氧化酶是一类重要的酶,它们主要利用 FAD 作为辅助因子参与氨基酸的氧化。其中许多酶在氨基酸的分解代谢中具有更广泛的底物特异性。另一方面,基于最近成功地将这些酶用于具有新辅助因子和机制的诊断,已经从自然界中筛选出了高度选择性的酶,并且通过 X 射线晶体学发现并进一步表征了许多新酶。作为具有生物合成或抗生素功能的氨基酸氧化酶的筛选结果,发现了 l-Trp 氧化酶、l-Lys 氧化酶和 Gly 氧化酶。依赖吡哆醛磷酸的 l-Arg 氧化酶具有羟基化未激活的 CC 键的新有趣活性。通过 d-氨基酸氧化酶的蛋白质工程创建了一种新的胺氧化酶。总结了氨基酸氧化酶的特性及其应用的最新进展。

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