Structural highlights
Function[ACOX3_YARLI] Oxidizes aliphatic acyl-CoA substrates of different chain lengths such as hexanoyl-CoA, decanoyl-CoA and myristyl-CoA as well as aromatic/heterocyclic ring-substituted chromogenic substrates, such as furylpropionyl-CoA. Of the above substrates, the efficiency of the enzyme, exhibits the following order: decanoyl-CoA > myristyl-CoA > hexanoyl-CoA > furyl-propionyl-CoA. Publication Abstract from PubMedAcyl-CoA oxidases (ACOXs) play important roles in lipid metabolism, including peroxisomal fatty acid beta-oxidation by the conversion of acyl-CoAs to 2-trans-enoyl-CoAs. The yeast Yarrowia lipolyticacan utilize fatty acidsas a carbon source and thus has extensive biotechnological applications. The crystal structure of ACOX3from Y. lipolytica(YlACOX3) was determinedat a resolution of2.5 A. It contained two molecules per asymmetric unit, and the monomeric structure was folded into four domains, Nalpha, Nbeta, Calpha1 and Calpha2domains. The cofactor flavin adenine dinucleotide (FAD)was bound in the dimer interface. The substrate-binding pocket was located near the cofactor and formed at the interface between the Nalpha, Nbeta, and Calpha1 domains. Comparisons with the 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 to those of medium- and long-chain ACOXs, and the structural basis for their differences in substrate specificity was discussed. Crystal structure of acyl-CoA oxidase3from Yarrowia lipolyticawith specificity for short-chain acyl-CoA.,Kim S, Kim KJ J Microbiol Biotechnol. 2018 Feb 13. pii: 10.4014/jmb.1711.11032. doi:, 10.4014/jmb.1711.11032. PMID:29429324[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 05:55, 16 May 2018.