| Structural highlights
Function
OLEA_XANCP Involved in olefin biosynthesis (PubMed:21266575, PubMed:22524624, PubMed:27815501, PubMed:28223313). Catalyzes a non-decarboxylative head-to-head Claisen condensation of two acyl-CoA molecules, generating an (R)-2-alkyl-3-oxoalkanoate (PubMed:21266575, PubMed:22524624, PubMed:27815501). Is active with fatty acyl-CoA substrates that ranged from C(8) to C(16) in length, and is the most active with palmitoyl-CoA and myristoyl-CoA (PubMed:21266575).[1] [2] [3] [4]
Publication Abstract from PubMed
Renewable production of hydrocarbons is being pursued as a petroleum-independent source of commodity chemicals and replacement for biofuels. The bacterial biosynthesis of long-chain olefins represents one such platform. The process is initiated by OleA catalyzing the condensation of two fatty acyl-coenzyme A substrates to form a beta-keto acid. Here, the mechanistic role of the conserved His285 is investigated through mutagenesis, activity assays, and X-ray crystallography. Our data demonstrate that His285 is required for product formation, influences the thiolase nucleophile Cys143 and the acyl-enzyme intermediate before and after transesterification, and orchestrates substrate coordination as a defining component of an oxyanion hole. As a consequence, His285 plays a key role in enabling a mechanistic strategy in OleA that is distinct from other thiolases.
The role of OleA His285 in orchestration of long-chain acyl-coenzyme A substrates.,Jensen MR, Goblirsch BR, Esler MA, Christenson JK, Mohamed FA, Wackett LP, Wilmot CM FEBS Lett. 2018 Feb 11. doi: 10.1002/1873-3468.13004. PMID:29430657[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Frias JA, Richman JE, Erickson JS, Wackett LP. Purification and characterization of OleA from Xanthomonas campestris and demonstration of a non-decarboxylative Claisen condensation reaction. J Biol Chem. 2011 Apr 1;286(13):10930-8. doi: 10.1074/jbc.M110.216127. Epub 2011 , Jan 25. PMID:21266575 doi:http://dx.doi.org/10.1074/jbc.M110.216127
- ↑ Goblirsch BR, Frias JA, Wackett LP, Wilmot CM. Crystal Structures of Xanthomonas Campestris OleA Reveal Features That Promote Head-to-Head Condensation of Two Long-Chain Fatty Acids. Biochemistry. 2012 Apr 23. PMID:22524624 doi:10.1021/bi300386m
- ↑ Goblirsch BR, Jensen MR, Mohamed FA, Wackett LP, Wilmot CM. Substrate Trapping in Crystals of the Thiolase OleA Identifies Three Channels That Enable Long Chain Olefin Biosynthesis. J Biol Chem. 2016 Dec 23;291(52):26698-26706. doi: 10.1074/jbc.M116.760892. Epub , 2016 Nov 4. PMID:27815501 doi:http://dx.doi.org/10.1074/jbc.M116.760892
- ↑ Christenson JK, Jensen MR, Goblirsch BR, Mohamed F, Zhang W, Wilmot CM, Wackett LP. Active Multienzyme Assemblies for Long-Chain Olefinic Hydrocarbon Biosynthesis. J Bacteriol. 2017 Apr 11;199(9):e00890-16. doi: 10.1128/JB.00890-16. Print 2017 , May 1. PMID:28223313 doi:http://dx.doi.org/10.1128/JB.00890-16
- ↑ Jensen MR, Goblirsch BR, Esler MA, Christenson JK, Mohamed FA, Wackett LP, Wilmot CM. The role of OleA His285 in orchestration of long-chain acyl-coenzyme A substrates. FEBS Lett. 2018 Feb 11. doi: 10.1002/1873-3468.13004. PMID:29430657 doi:http://dx.doi.org/10.1002/1873-3468.13004
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