SPECIFICITY OF GUINEA-PIG LIVER TRANSGLUTAMINASE FOR AMINE SUBSTRATES
SPECIFICITY OF GUINEA-PIG LIVER TRANSGLUTAMINASE FOR AMINE SUBSTRATES
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DOI：
10.1021/bi00576a019
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发表时间：
1979-01-01
期刊：
影响因子：
2.9
通讯作者：
MOSES, P
中科院分区：
文献类型：
--
作者：
LORAND, L;PARAMESWARAN, KN;MOSES, P
用高表观亲和力的合成底物研究了内切-γ-谷氨酰胺：β-赖氨酸转移酶模型酶--豚鼠肝脏谷氨酰胺转氨酶的胺专一性。例如dansyl-(5-dimethylamino-1-naphthalenesulfonyl)，(2，4-二硝基苯磺酰基)-和(2，4，6-triisopropylbenzenesulfonyl)-cadaverines，，每个都表现出约4倍的亲和力。107/M时，最好的胺底物携带大的疏水取代基连接到长约7.2埃的烷基胺侧链上。在酶中存在疏水结合区，从那里烷基侧链向活性中心延伸到一个狭窄的缝隙中，并定位底物的伯胺以攻击酰基酶中间体的羰基。
The amine specificity of guinea pig liver transglutaminase, a model enzyme for endo-.gamma.-glutamine:.epsilon.-lysine transferases, was explored with the aid of synthetic substrates of high apparent affinities. As exemplified by dansyl-(5-dimethylamino-1-naphthalenesulfonyl), (2,4-dinitrobenzenesulfonyl)-, and (2,4,6-triisopropylbenzenesulfonyl)-cadaverines, each of which showed affinities of approximately 4 .times. 107/M, the best amine substrates carried a large hydrophobic substituent attached to an alkylamine side chain of about 7.2 .ANG. in length. A hydrophobic binding region exists in the enzyme from where the alkyl side chain reaches into a narrow crevice toward the active center and positions the primary amine of the substrate for attacking the carbonyl group of the acyl enzyme intermediate.