دورية أكاديمية
Structural and biochemical characterization of MCAT from photosynthetic microorganism Synechocystis sp. PCC 6803 reveal its stepwise catalytic mechanism.
| العنوان: | Structural and biochemical characterization of MCAT from photosynthetic microorganism Synechocystis sp. PCC 6803 reveal its stepwise catalytic mechanism. |
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| المؤلفون: | Liu Y; Marine Bioengineering Group, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China., Feng Y; Marine Bioengineering Group, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China., Wang Y; Marine Bioengineering Group, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China; University of Chinese Academy of Sciences, Beijing 100039, China., Li X; Dalian Polytechnic University, Dalian 116034, China., Cao X; Marine Bioengineering Group, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China., Xue S; Marine Bioengineering Group, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China. Electronic address: xuesong@dicp.ac.cn. |
| المصدر: | Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2015 Feb 13; Vol. 457 (3), pp. 398-403. Date of Electronic Publication: 2015 Jan 09. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1090-2104 (Electronic) Linking ISSN: 0006291X NLM ISO Abbreviation: Biochem Biophys Res Commun Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: <2002- >: San Diego, CA : Elsevier Original Publication: New York, Academic Press. |
| مواضيع طبية MeSH: | Acyl-Carrier Protein S-Malonyltransferase/*chemistry , Acyl-Carrier Protein S-Malonyltransferase/*metabolism , Bacterial Proteins/*chemistry , Bacterial Proteins/*metabolism , Synechocystis/*enzymology, Acyl-Carrier Protein S-Malonyltransferase/genetics ; Amino Acid Sequence ; Amino Acid Substitution ; Bacterial Proteins/genetics ; Catalysis ; Catalytic Domain ; Conserved Sequence ; Crystallography, X-Ray ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Conformation ; Sequence Homology, Amino Acid ; Synechocystis/genetics |
| مستخلص: | Malonyl-coenzyme A: acyl-carrier protein transacylase (MCAT) catalyzes the transfer of malonyl group from malonyl-CoA to the holo-acyl carrier protein (Holo-ACP), yielding malonyl-ACP. The overall reaction has been extensively studied in heterotrophic microorganisms, while its mechanism in photosynthetic autotrophs as well as the stepwise reaction information remains unclear. Here the 2.42 Å crystal structure of MCAT from photosynthetic microorganism Synechocystis sp. PCC 6803 is presented. It demonstrates that Arg113, Ser88 and His188 constitute catalytic triad. The second step involved ACP-MCAT-malonyl intermediate is speed-limited instead of the malonyl-CoA-MCAT intermediate in the first step. Therefore His87, Arg113 and Ser88 render different contributions for the two intermediates. Additionally, S88T mutant initializes the reaction by H87 deprotonating S88T which is different from the wild type. (Copyright © 2015 Elsevier Inc. All rights reserved.) |
| فهرسة مساهمة: | Keywords: Intermediate; MCAT; Structure; Synechocystis sp. PCC 6803 |
| المشرفين على المادة: | 0 (Bacterial Proteins) EC 2.3.1.39 (Acyl-Carrier Protein S-Malonyltransferase) |
| تواريخ الأحداث: | Date Created: 20150114 Date Completed: 20150709 Latest Revision: 20150216 |
| رمز التحديث: | 20240628 |
| DOI: | 10.1016/j.bbrc.2015.01.003 |
| PMID: | 25582772 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1090-2104 |
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| DOI: | 10.1016/j.bbrc.2015.01.003 |