A chymosin‐like extracellular acidic endoprotease from Myxococcus xanthus DK101

FEBS Letters

Cenatiempo, Yves¹  Vachon, Gilles¹  Raingeaud, Joël¹  Carias, Jean-Robert²  Mazaud, Catherine²  Lucas, Nathalie²  Julien, Raymond² 

[1] Laboratoires de biochimie cellulaire et de biologie moléculaire. Faculté des Sciences, 40 avenue du Recteur Pineau, 86022 Poitiers Cedex, France;Genius (Biotechnologie), Faculté des Sciences, 123 rue Albert Thomas. 87060 Limoges Cedex, France

关键词: Myxobacteria;    k-Casein;    Tripartite protein;    Rennin;    Protease;    (Myxococcus xanthus DK101);    DABTH;    4-N;    N-dimethylaminoazobenzene 4'-thiohydantoin;    TLC;    thin-layer chromatography;    ] CTT;    Casitone-Tris medium;    Nle;    Norleucine;    IPTG;    isopropyl β-D-thiogalactoside;   

DOI  :  10.1016/0014-5793(90)80162-C

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown