Voinarsky I N, Yarovenko V L
Prikl Biokhim Mikrobiol. 1975 Nov-Dec;11(6):835-41.
The specific action and composition of the functional groups of active centres of three fractions of acid proteinases from Aspergillus terricola have been studied. With respect to the hydrolysis rates of acetyl-L-phenylalanyl-L-tyrosine and carbobenzoxy-D, L-glycyl-phenylalanine by the three fractions it is suggested that the interaction of acid proteinases with the substrate involves hydrophobic forces. It has been shown that the above fractions are no metal enzymes. By means of the diazocarbonyl inhibitor an occurrence of a catalytically active carboxy group has been found in the active centre of proteinases. The proteinase inhibition by Fe3+ in the presence of citric acid is an indirect evidence of the existence of several carboxy groups and, possibly, of a hydroxy group in the active centre of acid proteinases from Aspergillus terricola.
对土栖曲霉酸性蛋白酶三个组分活性中心功能基团的具体作用和组成进行了研究。根据这三个组分对乙酰-L-苯丙氨酰-L-酪氨酸和苄氧羰基-D，L-甘氨酰-苯丙氨酸的水解速率，表明酸性蛋白酶与底物的相互作用涉及疏水力。已证明上述组分不是金属酶。通过重氮羰基抑制剂，在蛋白酶的活性中心发现了一个具有催化活性的羧基。在柠檬酸存在下Fe3+对蛋白酶的抑制作用间接证明了土栖曲霉酸性蛋白酶活性中心存在几个羧基，可能还存在一个羟基。
