2qve
From Proteopedia
Crystal Structure of SgTAM bound to mechanism based inhibitor
Structural highlights
FunctionTAM_STRGL Involved in the biosynthesis of the enediyne antitumor antibiotic C-1027. Catalyzes the MIO-dependent deamination of L-tyrosine generating the corresponding alpha,beta-unsaturated acid, (S)-beta-tyrosine.[1] [2] [3] 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 PubMedThe synthesis and evaluation of two classes of inhibitors for SgTAM, a 4-methylideneimidazole-5-one (MIO) containing tyrosine aminomutase, are described. A mechanism-based strategy was used to design analogs that mimic the substrate or product of the reaction and form covalent interactions with the enzyme through the MIO prosthetic group. The analogs were characterized by measuring inhibition constants and X-ray crystallographic structural analysis of the co-complexes bound to the aminomutase, SgTAM. Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase SgTAM.,Montavon TJ, Christianson CV, Festin GM, Shen B, Bruner SD Bioorg Med Chem Lett. 2008 May 15;18(10):3099-102. Epub 2007 Nov 19. PMID:18078753[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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