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Structural characterization of a Δ 3 , Δ 2 -enoyl-CoA isomerase from Pseudomonas aeruginosa: implications for its involvement in unsaturated fatty acid metabolism.
- Source :
-
Journal of biomolecular structure & dynamics [J Biomol Struct Dyn] 2019 Jul; Vol. 37 (10), pp. 2695-2702. Date of Electronic Publication: 2018 Nov 17. - Publication Year :
- 2019
-
Abstract
- Gene PA4980 from Pseudomonas aeruginosa encodes a putative enoyl-coenzyme A hydratase/isomerase that is associated with the function of the biofilm dispersion-inducing signal molecule cis-2-decenoic acid. To elucidate the role of PA4980 in cis-2-decenoic acid biosynthesis, we reported the crystal structure of its protein product at 2.39 Å. The structural analysis and substrate binding prediction suggest that it acts as a monofunctional enoyl-coenzyme A isomerase, implicating an alternative pathway of the cis-2-decenoic acid synthesis.
- Subjects :
- Amino Acid Sequence
Dodecenoyl-CoA Isomerase metabolism
Fatty Acids, Unsaturated chemistry
Fatty Acids, Unsaturated metabolism
Isomerases chemistry
Isomerases metabolism
Lipid Metabolism
Molecular Dynamics Simulation
Protein Array Analysis
Protein Binding
Structure-Activity Relationship
Dodecenoyl-CoA Isomerase chemistry
Models, Molecular
Protein Conformation
Pseudomonas aeruginosa enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1538-0254
- Volume :
- 37
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- Journal of biomolecular structure & dynamics
- Publication Type :
- Academic Journal
- Accession number :
- 30052139
- Full Text :
- https://doi.org/10.1080/07391102.2018.1495102