|
|
| Line 10: |
Line 10: |
| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/Q59713_PSEPU Q59713_PSEPU] | | [https://www.uniprot.org/uniprot/Q59713_PSEPU Q59713_PSEPU] |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
| |
| The X-ray crystal structure of a salicylate hydroxylase from Pseudomonas putida S-1 complexed with coenzyme FAD has been determined to a resolution of 2.5 A. Structural conservation with p- or m-hydroxybenzoate hydroxylase is very good throughout the topology, despite a low amino sequence identity of 20-40% between these three hydroxylases. Salicylate hydroxylase is composed of three distinct domains and includes FAD between domains I and II, which is accessible to solvent. In this study, which analyzes the tertiary structure of the enzyme, the unique reaction of salicylate, i.e. decarboxylative hydroxylation, and the structural roles of amino acids surrounding the substrate, are considered.
| |
|
| |
| The catalytic mechanism of decarboxylative hydroxylation of salicylate hydroxylase revealed by crystal structure analysis at 2.5 A resolution.,Uemura T, Kita A, Watanabe Y, Adachi M, Kuroki R, Morimoto Y Biochem Biophys Res Commun. 2015 Nov 23. pii: S0006-291X(15)30956-6. doi:, 10.1016/j.bbrc.2015.11.087. PMID:26616054<ref>PMID:26616054</ref>
| |
|
| |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| |
| </div>
| |
| <div class="pdbe-citations 5evy" style="background-color:#fffaf0;"></div>
| |
|
| |
|
| ==See Also== | | ==See Also== |
| *[[Hydroxylases 3D structures|Hydroxylases 3D structures]] | | *[[Hydroxylases 3D structures|Hydroxylases 3D structures]] |
| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
