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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.

Authors :
Liu L
Li T
Peng CT
Sun CZ
Li CC
Xiao QJ
He LH
Wang NY
Song YJ
Zhu YB
Li H
Kang M
Tang H
Xiong X
Bao R
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.

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