Abstract：
:Epoxide hydrolases (EH, EC 3.3.2.3) have been proposed to be key enzymes in the biosynthesis of polyether (PE) ladder compounds such as the brevetoxins which are produced by the dinoflagellate Karenia brevis. These enzymes have the potential to catalyze kinetically disfavored endo-tet cyclization reactions. Data mining of K. brevis transcriptome libraries revealed two classes of epoxide hydrolases: microsomal and leukotriene A4 (LTA4) hydrolases. A microsomal EH was cloned and expressed for characterization. The enzyme is a monomeric protein with molecular weight 44kDa. Kinetic parameters were evaluated using a variety of epoxide substrates to assess substrate selectivity and enantioselectivity, as well as its potential to catalyze the critical endo-tet cyclization of epoxy alcohols. Monitoring of EH activity in high and low toxin producing cultures of K. brevis over a three week period showed consistently higher activity in the high toxin producing culture implicating the involvement of one or more EH in brevetoxin biosynthesis.
journal_name
Phytochemistryjournal_title
Phytochemistryauthors
Sun P,Leeson C,Zhi X,Leng F,Pierce RH,Henry MS,Rein KSdoi
10.1016/j.phytochem.2015.11.002subject
Has Abstractpub_date
2016-02-01 00:00:00pages
11-21eissn
0031-9422issn
1873-3700pii
S0031-9422(15)30103-5journal_volume
122pub_type
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