KMID : 0545120180280040597
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Journal of Microbiology and Biotechnology 2018 Volume.28 No. 4 p.597 ~ p.605
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Crystal Structure of Acyl-CoA Oxidase 3 from Yarrowia lipolytica with Specificity for Short-Chain Acyl-CoA
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Kim Sang-Woo
Kim Kyung-Jin
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Abstract
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Acyl-CoA oxidases (ACOXs) play important roles in lipid metabolism, including peroxisomal fatty acid ¥â-oxidation by the conversion of acyl-CoAs to 2-trans-enoyl-CoAs. The yeast Yarrowia lipolytica can utilize fatty acids as a carbon source and thus has extensive biotechnological applications. The crystal structure of ACOX3 from Y. lipolytica (YlACOX3) was determined at a resolution of 2.5 A. It contained two molecules per asymmetric unit, and the monomeric structure was folded into four domains; N¥á, N¥â, C¥á1, and C¥á2 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 N¥á, N¥â, and C¥á1 domains. Comparisons with other ACOX structures provided structural insights into how YlACOX has a substrate preference for short-chain acyl-CoA. In addition, the structure of YlACOX3 was compared with those of medium- and long-chain ACOXs, and the structural basis for their differences in substrate specificity was discussed.
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KEYWORD
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Yarrowia lipolytica, acyl-CoA oxidase3, fatty acid, ¥â-oxidation
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