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B6db references: 93170282

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

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