13532-18-8Relevant articles and documents
A mechanistic rationalisation for the substrate specificity of recombinant mammalian 4-hydroxyphenylpyruvate dioxygenase (4-HPPD)
Crouch, Nicholas P.,Adlington, Robert M.,Baldwin, Jack E.,Lee, Meng -Huee,MacKinnon, Colin H.
, p. 6993 - 7010 (1997)
The isolation and purification of α-ketoisocaproate dioxygenase [α-KICD] from rat liver is described. Sequence determination of the purified protein revealed it to have complete homology to rat liver 4-hydroxyphenylpyruvate dioxygenase [4-HPPD] which was confirmed by the cloning and expression of the gene encoding 4-HPPD in E. coli. Examination of the substrate specificity of the resulting soluble recombinant protein revealed it to be capable of the oxidative decarboxylation of a range of ketoacids derived from proteinogenic amino acids. The significance of the turnover of these different ketoacids is discussed in relation to the mechanism of this fascinating enzyme.
Tressl et al.
, p. 455,457 (1977)
Methoxymethyl Cations. 2. Reactions with Allylic Ethers and Sulfides in the Gas Phase
Kim, Jhong K.,Bonicamp, Judith,Caserio, Marjorie C.
, p. 4236 - 4242 (1981)
Reactions of allylic compounds 3-methoxy-1-propene and 3-(methylthio)-1-propene with gaseous methoxymethyl cations generated from methyl ethers on electron impact have been investigated by ion cyclotron resonance techniques.Three modes of reaction have been identified for the allylic sulfide with CH3OCH2+ that correspond to the elimination of the elements of CH2=O, CH3OH, and CH3SH.The allylic ether and CH3OCH2+ reacted to eliminate CH3OH predominantly.Pathways for these reactions were studied by using isotopic labels.The results are interpreted in terms of attack of the reactant ion at the terminal carbon of the allyl group followed by hydride and/or proton transfers and elimination of CH2O, CH3OH, or CH3SH.Oxygen lost as the neutral arose predominantly but not exclusively by cleavage of the methylene-oxygen bond of the reactant ion.Methylthiolation of 3-(methylthio)-1-propene also was achieved by reaction with CH3OCH2+ in the presence of methyl disulfide.The score of a small amount of label scrambling in deuterium-labeled reactant ions is discussed.
Synthesis of Highly Enantioenriched Sulfonimidoyl Fluorides and Sulfonimidamides by Stereospecific Sulfur–Fluorine Exchange (SuFEx) Reaction
Greed, Stephanie,Briggs, Edward L.,Idiris, Fahima I. M.,White, Andrew J. P.,Lücking, Ulrich,Bull, James A.
supporting information, p. 12533 - 12538 (2020/09/16)
Sulfonimidamides present exciting opportunities as chiral isosteres of sulfonamides, with potential for additional directional interactions. Here, we present the first modular enantioselective synthesis of sulfonimidamides, including the first stereoselective synthesis of enantioenriched sulfonimidoyl fluorides, and studies on their reactivity. A new route to sulfonimidoyl fluorides is presented from solid bench-stable, N-Boc-sulfinamide (Boc=tert-butyloxycarbonyl) salt building blocks. Enantioenriched arylsulfonimidoyl fluorides are shown to be readily racemised by fluoride ions. Conditions are developed, which trap fluoride and enable the stereospecific reaction of sulfonimidoyl fluorides with primary and secondary amines (100 % es, es=enantiospecificity) generating sulfonimidamides with up to 99 % ee. Aryl and alkyl sulfonimidoyl fluoride reagents are suitable for mild late stage functionalisation reactions, exemplified by coupling with a selection of complex amines in marketed drugs.
Chemical differentiation of three DMSP lyases from the marine: Roseobacter group
Burkhardt, Immo,Lauterbach, Lukas,Brock, Nelson L.,Dickschat, Jeroen S.
supporting information, p. 4432 - 4439 (2017/07/10)
Dimethylsulfoniopropionate (DMSP) catabolism of marine bacteria plays an important role in marine and global ecology. The genome of Ruegeria pomeroyi DSS-3, a model organism from the Roseobacter group, harbours no less than three genes for different DMSP lyases (DddW, DddP and DddQ) that catalyse the degradation of DMSP to dimethyl sulfide (DMS) and acrylate. Despite their apparent similar function these enzymes show no significant overall sequence identity. In this work DddQ and DddW from R. pomeroyi and the DddP homolog from Phaeobacter inhibens DSM 17395 were functionally characterised and their substrate scope was tested using several synthetic DMSP analogues. Comparative kinetic assays revealed differences in the conversion of DMSP and its analogues in terms of selectivity and overall velocity, giving additional insights into the molecular mechanisms of DMSP lyases and into their putatively different biological functions.
