The dacA gene of Bacillus stearothermophilus coding for d-alanine carboxypeptidase: cloning, structure and expression in Escherichia coli and Pichia pastoris
- 6 September 1993
- Vol. 131 (1) , 35-41
- https://doi.org/10.1016/0378-1119(93)90666-q
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Isolation and sequence analysis of dacB, which encodes a sporulation-specific penicillin-binding protein in Bacillus subtilisJournal of Bacteriology, 1992
- Yeast Systems for the Commercial Production of Heterologous ProteinsBio/Technology, 1991
- Mutations of the α-galactosidase signal peptide which greatly enhance secretion of heterologous proteins by yeastGene, 1991
- [12] High-efficiency transformation of yeast by electroporationPublished by Elsevier ,1991
- [34] α-Factor leader-directed secretion of heterologous proteins from yeastPublished by Elsevier ,1990
- Primary structure of the Streptomyces R61 extracellular DD‐peptidaseEuropean Journal of Biochemistry, 1987
- Active-site-serine d-alanyl-d-alanine-cleaving-peptidase-catalysed acyl-transfer reactions. Procedures for studying the penicillin-binding proteins of bacterial plasma membranesBiochemical Journal, 1986
- Hydrophobicity and amphiphilicity in protein structureJournal of Cellular Biochemistry, 1986
- Versatile expression vectors for high-level synthesis of cloned gene products in Escherichia coliGene, 1985
- Streptomyces R61 dd-carboxypeptidase: Hydrolysis of X-d-alanyl-d-alanine peptides measured by a fluorometric assayAnalytical Biochemistry, 1984