University of Sfax, ENIS, Laboratory of Biochemistry and Enzymatic Engineering of Lipases, Road of Soukra, BPW 1173-3038 Sfax, Tunisia.
UAB, Universitat Autònoma de Barcelona, Departament d'Enginyeria Química, Biològica i Ambiental, Bellaterra Barcelona, Spain.
Biomed Res Int. 2020 Mar 13;2020:3064290. doi: 10.1155/2020/3064290. eCollection 2020.
A full-length cDNA encoding digestive lipase (SmDL) was cloned from the pancreas of the smooth-hound (). The obtained cDNA was 1350 bp long encoding 451 amino acids. The deduced amino acid sequence has high similarity with known pancreatic lipases. Catalytic triad and disulphide bond positions are also conserved. According to the established phylogeny, the SmDL was grouped with those of tuna and lipases into one fish digestive lipase cluster. The recently purified enzyme shows no dependence for bile salts and colipase. For this, the residue-level interactions between lipase-colipase are yet to be clearly understood. The structural model of the SmDL was built, and several dissimilarities were noticed when analyzing the SmDL amino acids corresponding to those involved in HPL binding to colipase. Interestingly, the C-terminal domain of SmDL which holds the colipase shows a significant role for colipase interaction. This is apt to prevent the interaction between fish lipase and the pancreatic colipase which and can provide more explanation on the fact that the classical colipase is unable to activate the SmDL.
从灰星鲨的胰腺中克隆出全长 cDNA 编码消化脂肪酶（SmDL）。获得的 cDNA 长 1350bp，编码 451 个氨基酸。推导的氨基酸序列与已知的胰腺脂肪酶具有高度相似性。催化三联体和二硫键位置也保守。根据已建立的系统发育树，SmDL 与金枪鱼和脂肪酶一起分为鱼类消化脂肪酶簇。最近纯化的酶不依赖于胆汁盐和辅脂酶。对于这一点，脂肪酶-辅脂酶之间的残基相互作用仍有待清楚地了解。构建了 SmDL 的结构模型，并在分析与辅脂酶结合的 HPL 相关的 SmDL 氨基酸时注意到了几个差异。有趣的是，具有辅脂酶结合作用的 SmDL 的 C 末端结构域在辅脂酶相互作用中起着重要作用。这很可能阻止了鱼脂肪酶与胰腺辅脂酶之间的相互作用，并且可以更充分地解释经典辅脂酶无法激活 SmDL 的事实。
