Jiang W, Bond J S
Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg 24061.
FEBS Lett. 1992 Nov 9;312(2-3):110-4. doi: 10.1016/0014-5793(92)80916-5.
Crystal structures available for four metalloendopeptidases have revealed zinc ligands for these enzymes. New sequence information has made it possible to compare the primary structures of the zinc-binding site in metalloendopeptidases. A scheme based on the zinc-binding site is proposed to classify metalloendopeptidases into five distinct families: thermolysin, astacin, serratia, matrixin, and snake venom metalloproteinases. Two histidines and one glutamate are zinc-ligands in the thermolysin family. Three histidines and one tyrosine are zinc ligands in the other four families, which are further distinguished by the identity of the residue following the third histidine and by the environment surrounding the tyrosine.
已获得的四种金属内肽酶的晶体结构揭示了这些酶的锌配体。新的序列信息使得比较金属内肽酶中锌结合位点的一级结构成为可能。基于锌结合位点提出了一种方案,将金属内肽酶分为五个不同的家族:嗜热菌蛋白酶、龙虾肌碱蛋白酶、粘质沙雷氏菌蛋白酶、基质金属蛋白酶和蛇毒金属蛋白酶。在嗜热菌蛋白酶家族中,两个组氨酸和一个谷氨酸是锌配体。在其他四个家族中,三个组氨酸和一个酪氨酸是锌配体,这四个家族可根据第三个组氨酸之后的残基的一致性以及酪氨酸周围的环境进一步区分。