Bacterial L-serine dehydratases: a new family of enzymes containing iron-sulfur clusters.
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.
Grabowski
R
R
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität, Marburg, Germany.
Hofmeister
A E
AE
Buckel
W
W
D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000502:physiology; D012695:L-Serine Dehydratase / Q000737:chemistry* / Q000502:physiology; D010462:Peptostreptococcus / Q000201:enzymology*; D011732:Pyridoxal Phosphate; D013379:Substrate Specificity; D013913:Threonine Dehydratase / Q000737:chemistry
D007506:Iron-Sulfur Proteins; D011732:Pyridoxal Phosphate; D012695:L-Serine Dehydratase; D013913:Threonine Dehydratase