Graduate School of Pharmaceutical Sciences, Nagoya University, Chikusa, Japan.
Arch Biochem Biophys. 2013 Sep 1;537(1):138-43. doi: 10.1016/j.abb.2013.07.010. Epub 2013 Jul 19.
Transglutaminases are a family of enzymes that catalyze cross-linking reactions between proteins. Among the members, there is currently no information regarding the substrate preferences of transglutaminase 7 (TG7), that would clarify its physiological significance. We previously obtained several highly reactive substrate peptide sequences of transglutaminases from a random peptide library. In this study, we screened for preferred substrate sequences for TG7 from a phage-displayed 12-mer peptide library. The most preferred sequence was selected based on reactivity and isozyme specificity. We firstly exhibited the tendency for the preference of substrate sequence for TG7. Then, using the most efficient peptide, Z3S, we established an in vitro assay system to assess enzymatic activity of TG7.
转谷氨酰胺酶是一类能够催化蛋白质间发生交联反应的酶。目前,关于转谷氨酰胺酶 7(TG7)的底物偏好性尚无相关信息,这也使其生理意义尚不明确。我们之前曾从随机肽文库中获得了几种具有高反应活性的转谷氨酰胺酶的底物肽序列。在本研究中,我们从噬菌体展示的 12 肽文库中筛选了 TG7 的优先底物序列。根据反应活性和同工酶特异性选择最优先的序列。我们首先展示了 TG7 对底物序列偏好的趋势。然后,使用最有效的肽 Z3S,我们建立了体外测定体系来评估 TG7 的酶活性。