دورية أكاديمية
Kinetic and Structural Analysis of Two Linkers in the Tautomerase Superfamily: Analysis and Implications.
| العنوان: | Kinetic and Structural Analysis of Two Linkers in the Tautomerase Superfamily: Analysis and Implications. |
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| المؤلفون: | Baas BJ, Medellin BP, LeVieux JA, Erwin K, Lancaster EB, Johnson WH Jr, Kaoud TS, Moreno RY, de Ruijter M, Babbitt PC, Zhang YJ, Whitman CP |
| المصدر: | Biochemistry [Biochemistry] 2021 Jun 08; Vol. 60 (22), pp. 1776-1786. Date of Electronic Publication: 2021 May 21. |
| نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370623 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-4995 (Electronic) Linking ISSN: 00062960 NLM ISO Abbreviation: Biochemistry Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Washington, American Chemical Society. |
| مواضيع طبية MeSH: | Hydrolases/*chemistry , Isomerases/*chemistry, Amino Acid Sequence ; Binding Sites/physiology ; Catalysis ; Catalytic Domain/physiology ; Evolution, Molecular ; Kinetics ; Magnetic Resonance Spectroscopy/methods ; Models, Chemical |
| مستخلص: | The tautomerase superfamily (TSF) is a collection of enzymes and proteins that share a simple β-α-β structural scaffold. Most members are constructed from a single-core β-α-β motif or two consecutively fused β-α-β motifs in which the N-terminal proline (Pro-1) plays a key and unusual role as a catalytic residue. The cumulative evidence suggests that a gene fusion event took place in the evolution of the TSF followed by duplication (of the newly fused gene) to result in the diversification of activity that is seen today. Analysis of the sequence similarity network (SSN) for the TSF identified several linking proteins ("linkers") whose similarity links subgroups of these contemporary proteins that might hold clues about structure-function relationship changes accompanying the emergence of new activities. A previously uncharacterized pair of linkers (designated N1 and N2) was identified in the SSN that connected the 4-oxalocrotonate tautomerase (4-OT) and cis -3-chloroacrylic acid dehalogenase ( cis -CaaD) subgroups. N1, in the cis -CaaD subgroup, has the full complement of active site residues for cis -CaaD activity, whereas N2, in the 4-OT subgroup, lacks a key arginine (Arg-39) for canonical 4-OT activity. Kinetic characterization and nuclear magnetic resonance analysis show that N1 has activities observed for other characterized members of the cis -CaaD subgroup with varying degrees of efficiencies. N2 is a modest 4-OT but shows enhanced hydratase activity using allene and acetylene compounds, which might be due to the presence of Arg-8 along with Arg-11. Crystallographic analysis provides a structural context for these observations. |
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| معلومات مُعتمدة: | R01 GM125882 United States GM NIGMS NIH HHS; R01 GM129331 United States GM NIGMS NIH HHS; R01 GM104896 United States GM NIGMS NIH HHS; S10 OD021508 United States OD NIH HHS; R01 GM060595 United States GM NIGMS NIH HHS |
| المشرفين على المادة: | EC 3.- (Hydrolases) EC 3.8.1.- (cis-3-chloroacrylic acid dehalogenase) EC 5.- (4-oxalocrotonate tautomerase) EC 5.- (Isomerases) |
| تواريخ الأحداث: | Date Created: 20210521 Date Completed: 20211112 Latest Revision: 20211112 |
| رمز التحديث: | 20240628 |
| مُعرف محوري في PubMed: | PMC8257045 |
| DOI: | 10.1021/acs.biochem.1c00220 |
| PMID: | 34019384 |
| قاعدة البيانات: | MEDLINE |
Find this issue from the American Chemical Society | تدمد: | 1520-4995 |
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| DOI: | 10.1021/acs.biochem.1c00220 |