The essential oils of Syzygium aromaticum were isolated from its buds and leaves by hydrodistillation. The oils were analyzed by high resolution GC and GC-MS. Twenty-eight and 35 constituents representing 99.9% each were identified from the bud oils of Indian and Madagascan origins, respectively. On the other hand leaf oil from Madagascar resulted in the identification of 22 constituents representing 99.9% of the oil. The major constituents in bud and leaf oils were eugenol and β β β β β-caryophyllene.
Covalent linkers bridging the domains of multidomain proteins are considered to be crucial for assembly and function. In this report, an exception in which the linker of a two-domain dimeric L-asparaginase from Pyrococcus furiosus (PfA) was found to be dispensable is presented. Domains of this enzyme assembled without the linker into a conjoined tetrameric form that exhibited higher activity than the parent enzyme. The global shape and quaternary structure of the conjoined PfA were also similar to the wild-type PfA, as observed by their solution scattering profiles and X-ray crystallographic data. Comparison of the crystal structures of substrate-bound and unbound enzymes revealed an altogether new active-site composition and mechanism of action. Thus, conjoined PfA is presented as a unique enzyme obtained through noncovalent, linker-less assembly of constituent domains that is stable enough to function efficiently at elevated temperatures.
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