Structure of succinyl-CoA:3-ketoacid CoA transferase from Drosophila melanogaster

作者：Min Zhang, Han-Yang Xu, Yicui Wang, Zhubing Shi, Nannan Zhang · 发表于：Acta Crystallographica Section F Structural Biology and Crystallization Communications · 年份：2013 · DOI：10.1107/s1744309113024986 · 被引用次数：5 · 研究领域：Microbial Metabolic Engineering and Bioproduction、Enzyme Structure and Function、Biochemical and Molecular Research

Succinyl-CoA:3-ketoacid CoA transferase (SCOT) plays a crucial role in ketone-body metabolism. SCOT from Drosophila melanogaster (DmSCOT) was purified and crystallized. The crystal structure of DmSCOT was determined at 2.64 Å resolution and belonged to space group P212121, with unit-cell parameters a=76.638, b=101.921, c=122.457 Å, α=β=γ=90°. Sequence alignment and structural analysis identified DmSCOT as a class I CoA transferase. Compared with Acetobacter aceti succinyl-CoA:acetate CoA transferase, DmSCOT has a different substrate-binding pocket, which may explain the difference in their substrate specificities.