Saulnier J M, Curtil F M, Duclos M C, Wallach J M
Laboratoire de Biochimie Analytique, UA CNRS 244, Villeurbanne, France.
Biochim Biophys Acta. 1989 May 1;995(3):285-90. doi: 10.1016/0167-4838(89)90048-4.
Elastolysis of insoluble elastin by Pseudomonas aeruginosa elastase was found to be less specific (higher apparent Km value) but more active (higher activity) than with pancreatic elastase. Furthermore, pancreatic and P. aeruginosa elastases act synergistically during the initial stages of elastolysis. After extensive hydrolysis, the size distribution of digestion products was lower with P. aeruginosa than with pancreatic elastase. The higher extent of hydrolysis may be explained by the fact that, if pancreatic elastase needs at least six sub-sites for activity, P. aeruginosa elastase may hydrolyse tetrapeptides such as tetraalanine, or synthetic substrates such as furylacryloyltripeptides FA-X-Leu-Y, X and Y being Gly and/or Ala.
已发现铜绿假单胞菌弹性蛋白酶对不溶性弹性蛋白的弹性蛋白分解作用特异性较低（表观 Km 值较高），但比胰弹性蛋白酶更具活性（活性较高）。此外，胰弹性蛋白酶和铜绿假单胞菌弹性蛋白酶在弹性蛋白分解的初始阶段协同作用。经过广泛水解后，铜绿假单胞菌产生的消化产物的尺寸分布比胰弹性蛋白酶的更低。水解程度较高可能是因为，如果胰弹性蛋白酶发挥活性至少需要六个亚位点，那么铜绿假单胞菌弹性蛋白酶可能会水解四肽，如四丙氨酸，或合成底物，如呋喃丙烯酰三肽 FA-X-Leu-Y，其中 X 和 Y 为甘氨酸和/或丙氨酸。
