A CHYMOSIN-LIKE EXTRACELLULAR ACIDIC ENDOPROTEASE FROM MYXOCOCCUS-XANTHUS DK101 - A POTENTIAL NEW TOOL FOR PROTEIN ENGINEERING

被引：9

作者：

CARIAS, JR ^{[1
]}

RAINGEAUD, J ^{[1
]}

MAZAUD, C ^{[1
]}

VACHON, G ^{[1
]}

LUCAS, N ^{[1
]}

CENATIEMPO, Y ^{[1
]}

JULIEN, R ^{[1
]}

机构：

[1] FAC SCI POITIERS,BIOCHIM CELLULAIRE & BIOL MOLEC LAB,F-86022 POITIERS,FRANCE

来源：

FEBS LETTERS | 1990年 / 262卷 / 01期

关键词：

(Myxococcus xanthus DK101); k-Casein; Myxobacteria; Protease; Rennin; Tripartite protein;

D O I：

10.1016/0014-5793(90)80162-C

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：

SDS-PAGE and N-tenninal sequence analysis of hydrolysis products from 3 substrates containing a unique sensitive bond usually recognized by chymosin (k-casein, a synthetic hexapeptide and a recombinant tripartite protein) revealed that a 45 kDa endoprotease of Myxococcus xanthus DK101 cleaved the same characteristic Phe-Met bond with high specificity. Such an enzyme, easy to obtain from culture supernatant and to use in acidic conditions, could be a new tool for protein engineering. © 1990.

引用

页码：97 / 100

页数：4

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