PMID:8436113
| Citation |
Su, H, Moniakis, J and Newman, EB (1993) Use of gene fusions of the structural gene sdaA to purify L-serine deaminase 1 from Escherichia coli K-12. Eur. J. Biochem. 211:521-7 |
|---|---|
| Abstract |
The purification by affinity chromatography of beta-galactosidase from strains carrying sdaA/lacZ gene fusions results in the copurification of L-serine deaminase 1. We conclude that sdaA is the structural gene for the latter enzyme. The purified L-serine deaminase 1 obtained after collagenase treatment of an sdaA-collagen-lacZ fusion differs from the native enzyme by the addition of several amino acids at the C-terminal. Like the enzyme in crude extracts, this purified enzyme is catalytically inactive, and is activated by incubation with iron and dithiothreitol. |
| Links | |
| Keywords |
Base Sequence; Chromatography, High Pressure Liquid; Cloning, Molecular; Collagen/genetics; Collagenases/metabolism; Dithiothreitol/pharmacology; Enzyme Activation/drug effects; Escherichia coli/enzymology; Escherichia coli/genetics; Genes, Bacterial; Iron/pharmacology; L-Serine Dehydratase/genetics; L-Serine Dehydratase/isolation & purification; Molecular Sequence Data; Mutagenesis, Site-Directed; Plasmids; Recombinant Fusion Proteins/isolation & purification; Recombinant Fusion Proteins/metabolism; beta-Galactosidase/genetics; beta-Galactosidase/isolation & purification |
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