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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. Bacterial L-serine dehydratases: a new family of enzymes containing iron-sulfur clusters. Grabowski, R., Hofmeister, A.E., Buckel, W. Trends Biochem. Sci. (1993) [Pubmed]
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