Article
Purification, gene cloning, targeted knockout, overexpression, and biochemical characterization of the major pyrazinamidase from Mycobacterium smegmatis.
Journal of bacteriology - 1 Nov 1998
Boshoff H I, Mizrahi V
Abstract excerpt
The pyrazinamidase from Mycobacterium smegmatis was purified to homogeneity to yield a product of approximately 50 kDa. The deduced amino-terminal amino acid sequence of this polypeptide was used to design an oligonucleotide probe for screening a DNA library of M. smegmatis. An open reading frame...
Topics
- Amidohydrolases
- Amino Acid Sequence
- Animals
- Base Sequence
- Cloning, Molecular
- DNA, Bacterial
- Gene Expression
- Gene Targeting
- Mice
- Molecular Sequence Data
- Mutagenesis
- Mycobacterium smegmatis
- Mycobacterium tuberculosis
- Phenotype
