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酰基辅酶 A 氧化酶的特性研究来自脂肪分解酵母 SH14.

Characterization of Acyl-CoA Oxidases from the Lipolytic Yeast SH14.

机构信息

Synthetic Biology Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141, Republic of Korea.

Department of Biosystems and Bioengineering, KRIBB School of Biotechnology, Korea University of Science and Technology (UST), Daejeon 34113, Republic of Korea.

出版信息

J Microbiol Biotechnol. 2022 Jul 28;32(7):949-954. doi: 10.4014/jmb.2205.05029. Epub 2022 Jun 6.

Abstract

The lipolytic yeast SH14 contains three Acyl-CoA oxidases (ACOXs) which are encoded by the , , and genes and catalyze the first reaction in the β-oxidation of fatty acids. Here, the respective functions of the three isozymes were studied by growth analysis of mutant strains constructed by a combination of three mutations in minimal medium containing fatty acid as the sole carbon source. Substrate specificity of the isozymes was analyzed using recombinant SH14 strains overexpressing the respective genes. isozyme showed substrate specificity toward short- and medium-chain fatty acids (C6-C12), while isozyme preferred long-chain fatty acid longer than C12. isozyme revealed a preference for a broad substrate spectrum from C6-C16. Although the substrate specificity of and covers medium- and long-chain fatty acids, these two isozymes were insufficient for complete β-oxidation of long-chain fatty acids, and therefore was indispensable.

摘要

脂肪分解酵母 SH14 含有三种酰基辅酶 A 氧化酶(ACOXs),它们分别由基因、和编码,并催化脂肪酸β-氧化的第一步反应。在这里,通过在含有脂肪酸作为唯一碳源的最低培养基中构建三种突变的组合突变株的生长分析,研究了这三种同工酶的各自功能。使用过表达各自基因的重组 SH14 菌株分析了同工酶的底物特异性。同工酶对短链和中链脂肪酸(C6-C12)表现出底物特异性,而同工酶则偏爱长链脂肪酸,其长度大于 C12。同工酶显示出从 C6-C16 的宽底物谱的偏好。尽管同工酶和的底物特异性涵盖了中链和长链脂肪酸,但这两种同工酶不足以完全氧化长链脂肪酸,因此是必不可少的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/91d8/9628930/0f03f995de5d/jmb-32-7-949-f1.jpg

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