化学
内肽酶
双吖丙啶
氨基酸
残留物(化学)
亲和标签
立体化学
酶
谷氨酰胺
生物化学
谷氨酸脱氢酶
组合化学
连接器
谷氨酸受体
受体
计算机科学
操作系统
作者
Nlandu B. Bongo,Takenori Tomohiro,Y. Hatanaka
标识
DOI:10.1016/j.bmcl.2008.11.013
摘要
A novel photoreactive α-amino acid bearing an acidic residue and a cleavable diazirine was developed. To mimic common acidic α-amino acids, the residue was designed to be N-acylsulfonamide that possesses an acidic proton and is able to dissociate under the physiological conditions. The inhibition assay of its biotin-tagged derivative with glutamyl endopeptidase from Staphylococcus aureus V8 strain revealed a Kiapp value of 162 μM, which is slightly higher than the Km value of a common substrate. Upon UV irradiation, this derivative specifically photolabeled glutamyl endopeptidase, l-glutamate dehydrogenase, glutamic oxalacetic transaminase, and l-glutamine synthetase, all the enzymes exhibit high affinity toward acidic α-amino acids. In addition, N-acylsulfonamide group functioned as a cleavable linker in mild basic solution after a brief N-alkylation. Either the multifunctional nature or the simple structure of this acidic α-amino acid surrogate would be useful as versatile photoreactive building block.
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