Kim Sangwoo, Kim Kyung-Jin
School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University, Daegu 41566, Republic of Korea.
KNU Institute for Microorganisms, Kyungpook National University, Daegu 41566, Republic of Korea.
J Microbiol Biotechnol. 2018 Apr 28;28(4):597-605. doi: 10.4014/jmb.1711.11032.
Acyl-CoA oxidases (ACOXs) play important roles in lipid metabolism, including peroxisomal fatty acid β-oxidation by the conversion of acyl-CoAs to 2-trans-enoyl-CoAs. The yeast can utilize fatty acids as a carbon source and thus has extensive biotechnological applications. The crystal structure of ACOX3 from (ACOX3) was determined at a resolution of 2.5 Å. It contained two molecules per asymmetric unit, and the monomeric structure was folded into four domains; Nα, Nβ, Cα1, and Cα2 domains. The cofactor flavin adenine dinucleotide was bound in the dimer interface. The substrate-binding pocket was located near the cofactor, and formed at the interface between the Nα, Nβ, and Cα1 domains. Comparisons with other ACOX structures provided structural insights into how ACOX has a substrate preference for short-chain acyl-CoA. In addition, the structure of ACOX3 was compared with those of medium- and long-chain ACOXs, and the structural basis for their differences in substrate specificity was discussed.
酰基辅酶A氧化酶（ACOXs）在脂质代谢中发挥重要作用，包括通过将酰基辅酶A转化为2-反式烯酰基辅酶A进行过氧化物酶体脂肪酸β-氧化。酵母能够利用脂肪酸作为碳源，因此具有广泛的生物技术应用。测定了来自[具体来源未给出]的ACOX3（ACOX3）的晶体结构，分辨率为2.5 Å。每个不对称单元包含两个分子，单体结构折叠成四个结构域；Nα、Nβ、Cα1和Cα2结构域。辅因子黄素腺嘌呤二核苷酸结合在二聚体界面。底物结合口袋位于辅因子附近，在Nα、Nβ和Cα1结构域之间的界面处形成。与其他ACOX结构的比较为ACOX对短链酰基辅酶A具有底物偏好的原因提供了结构上的见解。此外，将ACOX3的结构与中链和长链ACOX的结构进行了比较，并讨论了它们在底物特异性上差异的结构基础。
