دورية أكاديمية
Evolution of substrate specificity within a diverse family of beta/alpha-barrel-fold basic amino acid decarboxylases: X-ray structure determination of enzymes with specificity for L-arginine and carboxynorspermidine.
| العنوان: | Evolution of substrate specificity within a diverse family of beta/alpha-barrel-fold basic amino acid decarboxylases: X-ray structure determination of enzymes with specificity for L-arginine and carboxynorspermidine. |
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| المؤلفون: | Deng X; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9041, USA., Lee J, Michael AJ, Tomchick DR, Goldsmith EJ, Phillips MA |
| المصدر: | The Journal of biological chemistry [J Biol Chem] 2010 Aug 13; Vol. 285 (33), pp. 25708-19. Date of Electronic Publication: 2010 Jun 08. |
| نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology |
| مواضيع طبية MeSH: | Evolution, Molecular*, Carboxy-Lyases/*chemistry , Carboxy-Lyases/*metabolism , Crystallography, X-Ray/*methods, Amino Acid Sequence ; Amino Acids, Basic/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Kinetics ; Molecular Sequence Data ; Protein Structure, Secondary ; Sequence Homology, Amino Acid ; Substrate Specificity |
| مستخلص: | Pyridoxal 5'-phosphate (PLP)-dependent basic amino acid decarboxylases from the beta/alpha-barrel-fold class (group IV) exist in most organisms and catalyze the decarboxylation of diverse substrates, essential for polyamine and lysine biosynthesis. Herein we describe the first x-ray structure determination of bacterial biosynthetic arginine decarboxylase (ADC) and carboxynorspermidine decarboxylase (CANSDC) to 2.3- and 2.0-A resolution, solved as product complexes with agmatine and norspermidine. Despite low overall sequence identity, the monomeric and dimeric structures are similar to other enzymes in the family, with the active sites formed between the beta/alpha-barrel domain of one subunit and the beta-barrel of the other. ADC contains both a unique interdomain insertion (4-helical bundle) and a C-terminal extension (3-helical bundle) and it packs as a tetramer in the asymmetric unit with the insertions forming part of the dimer and tetramer interfaces. Analytical ultracentrifugation studies confirmed that the ADC solution structure is a tetramer. Specificity for different basic amino acids appears to arise primarily from changes in the position of, and amino acid replacements in, a helix in the beta-barrel domain we refer to as the "specificity helix." Additionally, in CANSDC a key acidic residue that interacts with the distal amino group of other substrates is replaced by Leu(314), which interacts with the aliphatic portion of norspermidine. Neither product, agmatine in ADC nor norspermidine in CANSDC, form a Schiff base to pyridoxal 5'-phosphate, suggesting that the product complexes may promote product release by slowing the back reaction. These studies provide insight into the structural basis for the evolution of novel function within a common structural-fold. |
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| معلومات مُعتمدة: | R01 AI034432 United States AI NIAID NIH HHS; R37 AI034432 United States AI NIAID NIH HHS; R01AI34432 United States AI NIAID NIH HHS; R37AI34432 United States AI NIAID NIH HHS |
| سلسلة جزيئية: | PDB 3N29; 3N2O |
| المشرفين على المادة: | 0 (Amino Acids, Basic) 0 (Bacterial Proteins) EC 4.1.1.- (Carboxy-Lyases) EC 4.1.1.- (carboxynorspermidine decarboxylase) EC 4.1.1.19 (arginine decarboxylase) |
| تواريخ الأحداث: | Date Created: 20100611 Date Completed: 20100830 Latest Revision: 20211020 |
| رمز التحديث: | 20221213 |
| مُعرف محوري في PubMed: | PMC2919134 |
| DOI: | 10.1074/jbc.M110.121137 |
| PMID: | 20534592 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1083-351X |
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| DOI: | 10.1074/jbc.M110.121137 |