Dettori Léna, Ferrari Florent, Framboisier Xavier, Paris Cédric, Guiavarc'h Yann, Hôtel Laurence, Aymes Arnaud, Leblond Pierre, Humeau Catherine, Kapel Romain, Chevalot Isabelle, Aigle Bertrand, Delaunay Stéphane
Université de Lorraine CNRS LRGP Nancy France.
Université de Lorraine Plateau d'Analyse Structurale et Métabolomique Nancy France.
Eng Life Sci. 2018 May 21;18(8):589-599. doi: 10.1002/elsc.201700173. eCollection 2018 Aug.
The presence of aminoacylase activities was investigated in a crude extract of ATCC23877. First activities catalyzing the hydrolysis of N-α or ε-acetyl-L-lysine were identified. Furthermore, the acylation of lysine and different peptides was studied and compared with results obtained with lipase B of (CALB). Different regioselectivities were demonstrated for the two classes of enzymes. CALB was able to catalyze acylation only on the ε-position whereas the crude extract from possessed the rare ability to catalyze the N-acylation on the α-position of the lysine or of the amino-acid in N-terminal position of peptides. Two genes, and , were identified in the genome of ATCC23877 whose products show similarities with the previously identified aminoacylases from . The proteins encoded by these two genes were responsible for the major aminoacylase hydrolytic activities. Furthermore, we show that the hydrolysis of N-α-acetyl-L-lysine could be attributed to the product of gene.
对ATCC23877的粗提物中的氨酰化酶活性进行了研究。首先鉴定了催化N-α或ε-乙酰基-L-赖氨酸水解的活性。此外，还研究了赖氨酸和不同肽的酰化反应，并与来自（CALB）的脂肪酶B的结果进行了比较。这两类酶表现出不同的区域选择性。CALB仅能催化ε-位的酰化反应，而来自的粗提物具有罕见的能力，能够催化赖氨酸α-位或肽N端氨基酸的N-酰化反应。在ATCC23877的基因组中鉴定出两个基因，和，其产物与先前鉴定的来自的氨酰化酶具有相似性。这两个基因编码的蛋白质负责主要的氨酰化酶水解活性。此外，我们表明N-α-乙酰基-L-赖氨酸的水解可归因于基因的产物。
