Structural and functional characterization of β-cyanoalanine synthase from Tetranychus urticae
| Autor: | Daneshian, Leily, Renggli, Isabella, Hanaway, Ryan, Offermann, Lesa R., Schlachter, Caleb R., Hernandez Arriaza, Ricardo, Henry, Shannon, Prakash, Rahul, Wybouw, Nicky, Dermauw, Wannes, Shimizu, Linda S., Van Leeuwen, Thomas, Makris, Thomas M., Grbic, Vojislava, Grbic, Miodrag, Chruszcz, Maksymilian, 0000-0001-7521-5485 |
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| Rok vydání: | 2022 |
| Předmět: |
O-ACETYLSERINE SULFHYDRYLASE
beta-cyanoalanine synthase PHOTOCHEMICAL ACTIVITY Spider mite Lyases Biochemistry CYSTEINE SYNTHASE CYTOCHROME-OXIDASE MOLECULAR-BASIS ISOLATED CHLOROPLASTS Cyanide detoxification Animals CRYSTAL-STRUCTURE Cysteine Herbivory Cyanoalanine Molecular Biology Cyanides β-cyanoalanine synthase Biology and Life Sciences SULFIDE DETOXIFICATION Plants ALANINE SYNTHASE Insect Science CYANIDE Tetranychidae |
| Zdroj: | RIUR. Repositorio Institucional de la Universidad de La Rioja instname INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY |
| ISSN: | 0965-1748 1879-0240 |
| Popis: | Tetranychus urticae is a polyphagous spider mite that can feed on more than 1100 plant species including cyanogenic plants. The herbivore genome contains a horizontally acquired gene tetur10g01570 (TuCAS) that was previously shown to participate in cyanide detoxification. To understand the structure and determine the function of TuCAS in T. urticae, crystal structures of the protein with lysine conjugated pyridoxal phosphate (PLP) were determined. These structures reveal extensive TuCAS homology with the beta-substituted alanine synthase family, and they show that this enzyme utilizes a similar chemical mechanism involving a stable alpha-aminoacrylate intermediate in beta-cyanoalanine and cysteine synthesis. We demonstrate that TuCAS is more efficient in the synthesis of beta-cyanoalanine, which is a product of the detoxification reaction between cysteine and cyanide, than in the biosynthesis of cysteine. Also, the enzyme carries additional enzymatic activities that were not previously described. We show that TuCAS can detoxify cyanide using O-acetyl-L-serine as a substrate, leading to the direct formation of beta-cyanoalanine. Moreover, it catalyzes the reaction between the TuCAS-bound alpha-aminoacrylate intermediate and aromatic compounds with a thiol group. In addition, we have tested several compounds as TuCAS inhibitors. Overall, this study identifies additional functions for TuCAS and provides new molecular insight into the xenobiotic metabolism of T. urticae. |
| Databáze: | OpenAIRE |
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