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纯化的酵母天冬氨酸蛋白酶3在双碱性和单碱性位点切割角安康鱼前生长抑素I和II,以生成生长抑素-14和-28。

Purified yeast aspartic protease 3 cleaves anglerfish pro-somatostatin I and II at di- and monobasic sites to generate somatostatin-14 and -28.

作者信息

Cawley N X, Noe B D, Loh Y P

机构信息

Section on Cellular Neurobiology, National Institutes of Health, Bethesda, MD 20892.

出版信息

FEBS Lett. 1993 Oct 18;332(3):273-6. doi: 10.1016/0014-5793(93)80648-e.

Abstract

Anglerfish somatostatin-14 (SS-14) and somatostatin-28 (aSS-28) are derived from pro-somatostatin I (aPSS-I) and pro-somatostatin II (PSS-II), respectively. Purified yeast aspartic protease 3 (YAP3), was shown to cleave aPSS-I at the Arg81-Lys82 to yield SS-14 and Lys-1SS-14. In contrast, YAP3 cleaved aPSS-II only at the monobasic residue, Arg73 to yield aSS-28. Since the paired basic and monobasic sites are present in both precursors, the results indicate that the structure and conformation of these substrates dictate where cleavage occurs. Furthermore, the data show that YAP3 has specificity for both monobasic and paired basic residues.

摘要

琵琶鱼生长抑素-14(SS-14)和生长抑素-28(aSS-28)分别来源于前生长抑素I(aPSS-I)和前生长抑素II(PSS-II)。纯化的酵母天冬氨酸蛋白酶3(YAP3)可在精氨酸81-赖氨酸82处切割aPSS-I,产生SS-14和赖氨酸-1SS-14。相比之下,YAP3仅在单碱性残基精氨酸73处切割aPSS-II,产生aSS-28。由于这两种前体中都存在成对碱性和单碱性位点,结果表明这些底物的结构和构象决定了切割发生的位置。此外,数据显示YAP3对单碱性和成对碱性残基均具有特异性。

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