|
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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