Cloning and primary structure of the wide-spectrum amidase from Brevibacterium sp. R312: high homology to the amiE product from Pseudomonas aeruginosa
- 1 July 1992
- Vol. 116 (1) , 99-104
- https://doi.org/10.1016/0378-1119(92)90635-3
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Directed evolution of amidase in Methylophilus methylotrophus; purification and properties of amidases from wild-type and mutant strainsMicrobiology, 1991
- Primer-Directed Enzymatic Amplification of DNA with a Thermostable DNA PolymeraseScience, 1988
- The amino acid sequence of the aliphatic amidase from Pseudomonas aeruginosaFEBS Letters, 1987
- Chemical synthesis of a gene coding for human angiogenin, its expression in Escherichia coli and conversion of the product into its active formGene, 1987
- Purification and properties of an acylamide amidohydrolase (E. C. 3.5.1.4) with a wide activity spectrum from Brevibacterium sp. R 312Journal of Basic Microbiology, 1986
- Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectorsGene, 1985
- Activity and regulation of an amidase (acylamide amidohydrolase, EC 3.5.1.4) with a wide substrate spectrum from a Brevibacterium sp.Archiv für Mikrobiologie, 1984
- The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primersGene, 1982
- Purification and characterization of amidase which participates in nitrile degradation.Agricultural and Biological Chemistry, 1982
- Biochemical and Immunological Comparison of Aliphatic Amidases Produced by Pseudomonas SpeciesJournal of General Microbiology, 1972