Isobe K, Aumann K D, Schmid R D
Enzyme Technology Division, GBF-Gesellschaft für Biotechnologische Forschung, Braunschweig, Germany.
J Biotechnol. 1994 Jan 15;32(1):83-8. doi: 10.1016/0168-1656(94)90123-6.
The amino acid sequence of lipase from Penicillium camembertii was aligned with Rhizomucor miehei lipase without permitting any deletion or insertion in the structurally conserved regions. This lipase was classified into the R. miehei lipase family, because 33% of the residues were identical and 18% of the exchanges were conserved. A graphic molecular model for P. camembertii lipase was built using information from the sequence and X-ray structure of R. miehei lipase. The primary specificity pocket in the model of P. camembertii lipase predicted a substrate preference for monoacylglycerols and diacylglycerols. The close region to reactive His259 in P. camembertii lipase, which located in the opposite shore to the helical lid that was predictable to move in the activated state, contributed to the decision of the unique substrate specificity.
将卡门柏青霉脂肪酶的氨基酸序列与米黑根毛霉脂肪酶进行比对，在结构保守区域不允许任何缺失或插入。这种脂肪酶被归类到米黑根毛霉脂肪酶家族，因为33%的残基相同，18%的置换是保守的。利用米黑根毛霉脂肪酶的序列和X射线结构信息构建了卡门柏青霉脂肪酶的图形分子模型。卡门柏青霉脂肪酶模型中的主要特异性口袋预测其对单酰甘油和二酰甘油具有底物偏好性。卡门柏青霉脂肪酶中与活性His259相邻的区域，位于预测在活化状态下会移动的螺旋盖的对岸，这有助于决定其独特的底物特异性。
