3a15
Crystal Structure of Substrate-Free Form of Aldoxime Dehydratase (OxdRE)
Structural highlights
FunctionOXD_RHOER Catalyzes the dehydration of aldoximes to their corresponding nitrile (PubMed:16233624, PubMed:19740758). Is active toward various arylalkyl- and alkyl-aldoximes, and to a lesser extent toward aryl-aldoximes (PubMed:16233624).[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAldoxime dehydratase (Oxd) catalyzes the dehydration of aldoximes (R-CH=N-OH) to their corresponding nitrile (R-C triple bond N). Oxd is a heme-containing enzyme that catalyzes the dehydration reaction as its physiological function. We have determined the first two structures of Oxd: the substrate-free OxdRE at 1.8 A resolution and the n-butyraldoxime- and propionaldoxime-bound OxdREs at 1.8 and 1.6 A resolutions, respectively. Unlike other heme enzymes, the organic substrate is directly bound to the heme iron in OxdRE. We determined the structure of the Michaelis complex of OxdRE by using the unique substrate binding and activity regulation properties of Oxd. The Michaelis complex was prepared by x-ray cryoradiolytic reduction of the ferric dead-end complex in which Oxd contains a Fe(3+) heme form. The crystal structures reveal the mechanism of substrate recognition and the catalysis of OxdRE. X-ray crystal structure of michaelis complex of aldoxime dehydratase.,Sawai H, Sugimoto H, Kato Y, Asano Y, Shiro Y, Aono S J Biol Chem. 2009 Nov 13;284(46):32089-96. Epub 2009 Sep 8. PMID:19740758[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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