|
type |
Journal Article |
authors |
Grabowski, R.; Hofmeister, A. E.; Buckel, W. |
title |
Bacterial L-serine dehydratases: a new family of enzymes containing iron-sulfur clusters |
journal |
Trends Biochem Sci |
Activity |
4.3.1.17 |
sel |
selected |
ui |
8236444 |
year |
(1993) |
volume |
18 |
number |
8 |
pages |
297-300 |
| |
keywords |
Iron-Sulfur Proteins/*chemistry/physiology |
abstract |
Two families of enzymes are described which catalyse identical chemical reactions but differ in their prosthetic groups and hence in their mechanism of action. One family, the pyridoxal-5'-phosphate (PLP)- dependent L-threonine dehydratases, also use L-serine as substrate. The other, hitherto unrecognized family is the iron-dependent, highly specific bacterial L-serine dehydratases. It has been shown that L- serine dehydratase from the anaerobic bacterium Peptostreptococcus asaccharolyticus contains an iron-sulfur cluster but no PLP. A mechanism for the dehydration of L-serine which is similar, but not identical, to that of the dehydration of citrate catalysed by aconitase is proposed. |
last changed |
2009/06/29 12:45 |
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