The precursor of the Streptomyces R61 DD‐peptidase containing a C‐terminal extension is inactive

FEBS Letters

Bellefroid-Bourguignon, Catherine²  Wilkin, Jean-Marc²  Joris, Bernard²  Van Beeumen, Jozef¹  Ghuysen, Jean-Marie²  Komives, Elisabeth³  Frère, Jean-Marie²  Granier, Benoît²  Fanuel, Laurence²  Knowles, Jeremy³ 

[1] Vakgroep Biochemie, Fysiologie en Microbiologie, Rijksuniversiteit-Gent, K.L. Ledeganckstraat 35, 9000 Gent, Belgium;Laboratoire d'Enzymologie et Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, B6, B-4000 Sart-Tilman, Belgium;Department of Chemistry, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA

关键词: DD-peptidase;    Post-translational processing;    Protein maturation;    Heterologous expression;    Streptomyces;    LMM;    low molecular mass;    HMM;    high molecular mass;    Ac2- l-Lys-d-Ala-d-Ala;    N α;    N ε-diacetyl-l-lysyl-d-alanyl-d-alanine. Enzymes: DD-peptidase from Streptomyces R61 = EC 3.4.16.4. Lysozyme = EC 3.2.1.17;   

DOI  :  10.1016/0014-5793(94)00822-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The Streptomyces R61 DD-peptidase gene encodes a 26-residue C-terminal extension which is not found in the mature protein. When the gene was expressed in Escherichia coli, the extension was not cleaved and the precursor protein was not enzymatically active. It also reacted with penicillins significantly more slowly than the mature protein. The introduction of a ‘stop’ codon after that corresponding to the C-terminal residue of the mature protein resulted in the production of an active protein in the periplasm of E. coli.

【 授权许可】

Unknown