PURIFIED YEAST ASPARTIC PROTEASE-3 CLEAVES ANGLERFISH PRO-SOMATOSTATIN-I AND PRO-SOMATOSTATIN-II AT DIBASIC AND MONOBASIC SITES TO GENERATE SOMATOSTATIN-14 AND SOMATOSTATIN-28

被引:32
作者
CAWLEY, NX
NOE, BD
LOH, YP
机构
[1] NICHHD, DEV NEUROBIOL LAB,CELLULAR NEUROBIOL SECT,BLDG 49, RM 5A38, BETHESDA, MD 20892 USA
[2] EMORY UNIV, SCH MED, DEPT ANAT & CELL BIOL, ATLANTA, GA 30322 USA
[3] UNIFORMED SERV UNIV HLTH SCI, DEPT BIOCHEM, BETHESDA, MD 20814 USA
来源
FEBS LETTERS | 1993年 / 332卷 / 03期
关键词
PRO-SOMATOSTATIN; YEAST; ASPARTIC PROTEASE; PROHORMONE PROCESSING; SOMATOSTATIN;
D O I
10.1016/0014-5793(93)80648-E
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:273 / 276
页数:4
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