Marinova Margarita, Dolashki Alexander, Altenberend Florian, Stevanovic Stefan, Voelter Wolfgang, Tchorbanov Bozhidar
Institute of Organic Chemistry with Centre of Phytochemistry, Bulgarian Academy of Sciences, Acad. G. Bonchev Str. 9, 1113 Sofia, Bulgaria.
Protein Pept Lett. 2009;16(2):207-12. doi: 10.2174/092986609787316333.
Chick-pea (Cicer arietinum L.) cotyledons are unique source of aminopeptidase - 8-9 U/g cotyledons was observed using L-leucine-p-nitroanilide as substrate. The aminopeptidase was purified (65 kDa, pI 4.8 ) reaching a specific activity of 220 U/mg at pH 7.0-7.2 and 35-40 degrees C. The determined constant of specificity k(cat)/K(m) during hydrolysis of N-unsubstituted amino acid-p-nitroanilides showed a decrease order: Phe>Leu>Pro>Ile>Val>Ala. The enzyme was strongly inhibited by p-chloromercuribenzoic acid as well as in a competitive rate by the antihypertensive peptides Ile-Pro-Pro and Val-Pro-Pro.
鹰嘴豆（Cicer arietinum L.）子叶是氨肽酶的独特来源——以L-亮氨酸对硝基苯胺为底物时，观察到每克子叶中含有8 - 9 U的氨肽酶。该氨肽酶经纯化后（65 kDa，pI 4.8），在pH 7.0 - 7.2以及35 - 40摄氏度条件下，比活性达到220 U/mg。在N-未取代氨基酸对硝基苯胺水解过程中测定的特异性常数k(cat)/K(m)呈现出以下递减顺序：苯丙氨酸>亮氨酸>脯氨酸>异亮氨酸>缬氨酸>丙氨酸。该酶受到对氯汞苯甲酸的强烈抑制，同时也受到降压肽异亮氨酸-脯氨酸-脯氨酸和缬氨酸-脯氨酸-脯氨酸的竞争性抑制。
