6jox
triosephosphate isomerase-scylla paramamosaintriosephosphate isomerase-scylla paramamosain
Structural highlights
FunctionTPIS_SCYPA Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis.[UniProtKB:P00939] It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids.[UniProtKB:P00939] Publication Abstract from PubMedThe triosephosphate isomerase (TIM), Scy p 8, is a crab allergen and shows cross-reactivity in the shellfish. Here, recombinant Scy p 8 was expressed, and its crystal structure was determined at a resolution of 1.8 A. The three-dimensional structure of Scy p 8 is primarily composed of a (beta/alpha)8-barrel motif prototype. Additionally, Scy p 8 showed cross-reactivity with high sequential and secondary structural identity among TIMs from shellfish species. The site-directed mutagenesis of critical amino acids of conformational epitopes was carried out, and the mutants of Trp 168 and Lys 237 to Ala reduced immunoglobulin E (IgE)-binding activity by approximately 30%, compared with wild-type TIM in an inhibition ELISA; however, it still induced basophil activation despite the interpatient variability between patients. These results can help to provide an accurate template for the analysis of the IgE binding and establish meaningful relationships between structure and allergenicity. Crystal Structure Analysis and Conformational Epitope Mutation of Triosephosphate Isomerase, a Mud Crab Allergen.,Xia F, Li MS, Liu QM, Liu M, Yang Y, Cao MJ, Chen GX, Jin T, Liu GM J Agric Food Chem. 2019 Nov 20;67(46):12918-12926. doi: 10.1021/acs.jafc.9b05279., Epub 2019 Nov 11. PMID:31668066[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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