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N,N'-Bis(3-methylbut-2-enyl)-N,N'-(1,4-phenylene)dibenzenesulfonamide.

ABSTRACT: The complete mol-ecule of the title compound, C(28)H(32)N(2)O(4)S(2), is generated by a crystallographic inversion centre. The dihedral angle between the central and pendant aromatic rings is 46.78 (7)°. The C(ar)-S-N-C(ar) (ar = aromatic) torsion angle is 73.64 (15)° and the bond-angle sum for the N atom is 350.4°. In the crystal, weak C-H⋯O inter-actions link the mol-ecules, forming a two-dimensional network lying parallel to the bc plane.

SUBMITTER: Ejaz

PROVIDER: S-EPMC3238938 | biostudies-literature |

REPOSITORIES: biostudies-literature

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4,4'-(4,5-dimethyl-1,2-phenylene)bis(2-methylbut-3-yn-2-ol): structural variation in vicinal dialkynols.

Project description:The structure of the title compound, C(18)H(22)O(2), contains two non-equivalent molecules which differ primarily in the location of the -OH groups on opposite sides or on the same side of the molecular plane. Inversion-symmetric pairs of molecules form intermolecular O-H...O hydrogen-bonded tetrameric synthons that link non-equivalent molecules into an approximately square double layer parallel to (-102). Recently reported fluorinated analogues [Kane, Meyers, Yu, Gerken & Etzkorn (2011). Eur. J. Org. Chem. pp. 2969-2980] have significantly different structures of varying complexity that incorporate intramolecular hydrogen bonding and suggest that further study of structure versus substituents in vicinal dialkynols could be fruitful.

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Project description:The title compound, [Sm(C(25)H(35)N(2))(C(14)H(24)Si(2))(C(4)H(8)O)]·C(7)H(8), was prepared by treatment of anhydrous samarium trichloride with a 1:1 mixture of in situ-prepared Li(DippForm) [DippFormH = N,N'-bis-(2,6-diisopropyl-phen-yl)methanimidamide] and Li(2)(COT'') [COT'' = 1,4-bis-(trimethyl-sil-yl)cyclo-octa-tetra-enyl] in tetra-hydro-furan (THF). Despite the presence of two very bulky ligands (COT'' and DippForm), the mol-ecule still contains one coordinated THF ligand. The overall coordination geometry around the Sm(III) atom resembles a three-legged piano-stool with the COT'' ligand being ?(8)-coordinated and the DippForm(-) anion acting as an N,N'-chelating ligand [Sm-N = 2.5555?(15) and 2.4699?(15)?Å]. The asymmetric unit also contains a disordered mol-ecule of toluene, the refined ratio of the two components being 0.80?(4):0.20?(4).

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Project description:IspG is an intriguing enzyme in bacteria, parasite, and plant isoprenoid biosynthesis, and its catalytic mechanism remains elusive. We report here the synthesis of (2R,3R)-4-hydroxy-3-methyl-2,3-epoxybutanyl diphosphate (Epoxy-HMBPP), a proposed intermediate in one of the frequently cited mechanistic models. We have also demonstrated that this epoxide analogue is a catalytically competent IspG substrate. This study represents the first mechanistic study of this important enzyme.

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Overexpression and Suppression of Artemisia annua 4-Hydroxy-3-Methylbut-2-enyl Diphosphate Reductase 1 Gene (AaHDR1) Differentially Regulate Artemisinin and Terpenoid Biosynthesis.

Project description:4-Hydroxy-3-methylbut-2-enyl diphosphate reductase (HDR) catalyzes the last step of the 2-C-methyl-D-erythritol 4- phosphate (MEP) pathway to synthesize isopentenyl pyrophosphate (IPP) and dimethylallyl diphosphate (DMAPP). To date, little is known regarding effects of an increase or a decrease of a HDR expression on terpenoid and other metabolite profiles in plants. In our study, an Artemisia annua HDR cDNA (namely AaHDR1) was cloned from leaves. Expression profiling showed that it was highly expressed in leaves, roots, stems, and flowers with different levels. Green florescence protein fusion and confocal microscope analyses showed that AaHDR1 was localized in chloroplasts. The overexpression of AaHDR1 increased contents of artemisinin, arteannuin B and other sesquiterpenes, and multiple monoterpenes. By contrast, the suppression of AaHDR1 by anti-sense led to opposite results. In addition, an untargeted metabolic profiling showed that the overexpression and suppression altered non-polar metabolite profiles. In conclusion, the overexpression and suppression of AaHDR1 protein level in plastids differentially affect artemisinin and other terpenoid biosynthesis, and alter non-polar metabolite profiles of A. annua. Particularly, its overexpression leading to the increase of artemisinin production is informative to future metabolic engineering of this antimalarial medicine.

| S-EPMC5281613 | biostudies-literature

The amino-terminal conserved domain of 4-hydroxy-3-methylbut-2-enyl diphosphate reductase is critical for its function in oxygen-evolving photosynthetic organisms.

Project description:4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HDR), also known as isoprenoid synthesis H (IspH) or lysis-tolerant B (LytB), catalyzes the last step of the methylerythritol phosphate pathway to synthesize isopentenyl diphosphate and dimethylallyl diphosphate. The structure and reaction mechanism of IspH have been actively investigated in Escherichia coli but little is known in plants. Compared with the bacterial IspH, cyanobacterial and plant HDRs all contain an extra N-terminal conserved domain (NCD) that is essential for their function. Tyr72 in the NCD and several plant-specific residues around the central active site are critical for Arabidopsis HDR function. These results suggest that the structure and reaction mechanism of HDR/IspH may be different between plants and bacteria. The E. coli IspH is an iron-sulfur protein that is sensitive to oxygen. It is possible that the cyanobacterial HDR may independently evolve from the common ancestor of prokaryotes to obtain the NCD, which may protect the enzyme from high concentration of oxygen during photosynthesis.

| S-EPMC4622703 | biostudies-literature

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