Use of gene fusions of the structural gene sdaA to purify L-serine deaminase 1 from Escherichia coli K-12.

Eur. J. Biochem.1993 Feb 01;211(3):521-7. doi:10.1111/j.1432-1033.1993.tb17578.x

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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.

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Use of gene fusions of the structural gene sdaA to purify L-serine deaminase 1 from Escherichia coli K-12.

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