4kkv

Crystal structure of candida glabrata FMN adenylyltransferase D181A Mutant

spinqualitylabelsall models 4kkv, resolution 1.74Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4kkv is a 1 chain structure with sequence from Candida glabrata CBS 138. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.74Å Ligands: BGC, CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6FNA9_CANGA Publication Abstract from PubMed FMN adenylyltransferase (FMNAT) is an essential enzyme catalyzing the last step of a two-step pathway converting riboflavin (vitamin B2) to FAD, the ubiquitous flavocoenzyme. A structure-based mutagenesis and steady-state kinetic analysis of yeast FMNAT unexpectedly revealed that mutant D181A had a much faster turnover rate than the wild-type enzyme. Product inhibition analysis showed that wild-type FMNAT is strongly inhibited by FAD, whereas the D181A mutant has an attenuated product inhibition. These results provide a structural basis for the product inhibition of the enzyme and suggest that product release may be the rate-limiting step of the reaction. The "Super Mutant" of Yeast FMN Adenylyltransferase Enhances the Enzyme Turnover Rate by Attenuating Product Inhibition.,Huerta C, Grishin NV, Zhang H Biochemistry. 2013 May 15. PMID:23663086 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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