دورية أكاديمية
Exploring the Substrate Switch Motif of Aromatic Ammonia Lyases.
| العنوان: | Exploring the Substrate Switch Motif of Aromatic Ammonia Lyases. |
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| المؤلفون: | Brack Y; Department of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Straße 4, 17489, Greifswald, Germany., Sun C; Department of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Straße 4, 17489, Greifswald, Germany., Yi D; Department of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Straße 4, 17489, Greifswald, Germany.; Department of Biopharmaceuticals, China State Institute of Pharmaceutical Industry, Gebaini Road 285, 201203, Shanghai, P. R. China., Bornscheuer UT; Department of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Straße 4, 17489, Greifswald, Germany. |
| المصدر: | Chembiochem : a European journal of chemical biology [Chembiochem] 2023 Dec 01; Vol. 24 (23), pp. e202300584. Date of Electronic Publication: 2023 Oct 12. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Wiley-VCH Verlag Country of Publication: Germany NLM ID: 100937360 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1439-7633 (Electronic) Linking ISSN: 14394227 NLM ISO Abbreviation: Chembiochem Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Weinheim, Germany : Wiley-VCH Verlag, c2000- |
| مواضيع طبية MeSH: | Lyases*/metabolism , Ammonia-Lyases*/chemistry, Phenylalanine Ammonia-Lyase/chemistry ; Amino Acids/metabolism ; Phenylalanine ; Tyrosine ; Substrate Specificity |
| مستخلص: | Aromatic ammonia lyases (AALs) are important enzymes for biocatalysis as they enable the asymmetric synthesis of chiral l-α-amino acids from the corresponding α,β-unsaturated precursors. AALs have very similar protein structures and active site pockets but exhibit strict substrate specificity towards tyrosine, phenylalanine, or histidine. Herein, through systematic bioinformatics and structural analysis, we discovered eight new motifs of amino acid residues in AALs. After introducing them - as well as four already known motifs - into different AALs, we learned that altering the substrate specificity by engineering the substrate switch motif in phenylalanine ammonia lyases (PALs), phenylalanine/tyrosine ammonia lyases (PTALs), and tyrosine ammonia lyases (TALs) was only partially successful. However, we discovered that three previously unknown residue combinations introduced a substrate switch from tyrosine to phenylalanine in TAL, which was converted up to 20-fold better compared to the wild-type TAL enzyme. (© 2023 The Authors. ChemBioChem published by Wiley-VCH GmbH.) |
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| معلومات مُعتمدة: | 814650 European Union |
| فهرسة مساهمة: | Keywords: aromatic ammonia lyases; biocatalysis; bioinformatics analysis; substrate specificity; substrate switch motif |
| المشرفين على المادة: | EC 4.- (Lyases) EC 4.3.1.- (Ammonia-Lyases) EC 4.3.1.24 (Phenylalanine Ammonia-Lyase) 0 (Amino Acids) 47E5O17Y3R (Phenylalanine) 42HK56048U (Tyrosine) |
| تواريخ الأحداث: | Date Created: 20230925 Date Completed: 20231204 Latest Revision: 20240326 |
| رمز التحديث: | 20240326 |
| DOI: | 10.1002/cbic.202300584 |
| PMID: | 37747300 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1439-7633 |
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| DOI: | 10.1002/cbic.202300584 |