type	Journal Article
authors	Su, H.; Moniakis, J.; Newman, E. B.
title	Use of gene fusions of the structural gene sdaA to purify L-serine deaminase 1 from Escherichia coli K-12
journal	Eur J Biochem
Activity	4.3.1.17
ui	93170282
year	(1993)
volume	211
number	3
pages	521-7.
keywords	Base Sequence
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.
last changed	2002/11/18 17:04