From The Cover: SyrB2 in syringomycin E biosynthesis is a nonheme FeII -ketoglutarate- and O2-dependent halogenase
نویسندگان
چکیده
منابع مشابه
SyrB2 in syringomycin E biosynthesis is a nonheme FeII -ketoglutarate- and O2-dependent halogenase
The nine-residue lipodepsipeptide syringomycin E, elaborated as a phytotoxin by Pseudomonas syringae pv. syringae B301D contains a 4-Cl-L-Thr-9 moiety where failure to chlorinate results in a 3-fold drop in biological activity. The proteins SyrB1 and SyrB2 encoded by the biosynthetic cluster are shown to act as a substrate and enzyme pair for SyrB2-mediated chlorination of the aminoacyl-Senzyme...
متن کاملSyrB2 in syringomycin E biosynthesis is a nonheme FeII alpha-ketoglutarate- and O2-dependent halogenase.
The nine-residue lipodepsipeptide syringomycin E, elaborated as a phytotoxin by Pseudomonas syringae pv. syringae B301D contains a 4-Cl-L-Thr-9 moiety where failure to chlorinate results in a 3-fold drop in biological activity. The proteins SyrB1 and SyrB2 encoded by the biosynthetic cluster are shown to act as a substrate and enzyme pair for SyrB2-mediated chlorination of the aminoacyl-S-enzym...
متن کاملConformational switch triggered by alpha-ketoglutarate in a halogenase of curacin A biosynthesis.
The CurA halogenase (Hal) catalyzes a cryptic chlorination leading to cyclopropane ring formation in the synthesis of the natural product curacin A. Hal belongs to a family of enzymes that use Fe(2+), O(2) and alpha-ketoglutarate (alphaKG) to perform a variety of halogenation reactions in natural product biosynthesis. Crystal structures of the enzyme in five ligand states reveal strikingly diff...
متن کاملWhy does the enzyme SyrB2 chlorinate, but does not hydroxylate, saturated hydrocarbons? A density functional theory (DFT) study.
Syringomycin halogenase (SyrB2) is a non-heme Fe(II)/alpha-ketoglutarate (alphaKG)-dependent enzyme which catalyses halogenation of saturated hydrocarbons, but unlike other closely related enzymes, does not catalyse the corresponding hydroxylation reaction. We have carried out density functional theory (DFT) calculations to try to understand this specificity. Calculations which include only the...
متن کاملSubstrate positioning controls the partition between halogenation and hydroxylation in the aliphatic halogenase, SyrB2.
The alpha-ketoglutarate-dependent hydroxylases and halogenases employ similar reaction mechanisms involving hydrogen-abstracting Fe(IV)-oxo (ferryl) intermediates. In the halogenases, the carboxylate residue from the His(2)(Asp/Glu)(1) "facial triad" of iron ligands found in the hydroxylases is replaced by alanine, and a halide ion (X(-)) coordinates at the vacated site. Halogenation is thought...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2005
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0504412102