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B6db references: 8236444

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
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

B6db references