Structural highlights
Function
ETR1_CANTR Required for respiration and the maintenance of the mitochondrial compartment. May have a role in the mitochondrial synthesis of fatty acids.[1]
Publication Abstract from PubMed
An improved understanding of enzymes' catalytic proficiency and stereoselectivity would further enable applications in chemistry, biocatalysis and industrial biotechnology. We use a chemical probe to dissect individual catalytic steps of enoyl-thioester reductases (Etrs), validating an active site tyrosine as the cryptic proton donor and explaining how it had eluded definitive identification. This information enabled the rational redesign of Etr, yielding mutants that create products with inverted stereochemistry at wild type-like turnover frequency.
The use of ene adducts to study and engineer enoyl-thioester reductases.,Rosenthal RG, Vogeli B, Quade N, Capitani G, Kiefer P, Vorholt JA, Ebert MO, Erb TJ Nat Chem Biol. 2015 Apr 13. doi: 10.1038/nchembio.1794. PMID:25867044[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Torkko JM, Koivuranta KT, Miinalainen IJ, Yagi AI, Schmitz W, Kastaniotis AJ, Airenne TT, Gurvitz A, Hiltunen KJ. Candida tropicalis Etr1p and Saccharomyces cerevisiae Ybr026p (Mrf1'p), 2-enoyl thioester reductases essential for mitochondrial respiratory competence. Mol Cell Biol. 2001 Sep;21(18):6243-53. PMID:11509667
- ↑ Rosenthal RG, Vogeli B, Quade N, Capitani G, Kiefer P, Vorholt JA, Ebert MO, Erb TJ. The use of ene adducts to study and engineer enoyl-thioester reductases. Nat Chem Biol. 2015 Apr 13. doi: 10.1038/nchembio.1794. PMID:25867044 doi:http://dx.doi.org/10.1038/nchembio.1794
