55695-91-5Relevant articles and documents
Potent oligomerization and macrocyclization activity of the thioesterase domain of vicenistatin polyketide synthase
Kudo, Fumitaka,Asou, Yusaku,Watanabe, Moe,Kitayama, Takashi,Eguchi, Tadashi
, p. 1843 - 1846 (2012/08/29)
The thioesterase domain of the polyketide synthase involved in the biosynthesis of the 20-membered macrolactam antibiotic vicenistatin (VinTE) was found to catalyze oligomerization and macrocyclization of ω-hydroxy fatty acid ethyl esters to afford 17-28-membered macrocyclic lactones. The ring sizes of the macrocycles appear to be limited to the more moderate sizes because of the space limitation of the active site of VinTE. It was also verified that the initially formed linear dimer is first released from the active site of VinTE and then is recognized again by VinTE prior to its transformation to the cyclic dimer.
The synthesis of (11R,12S)-lactobacillic acid and its enantiomer
Coxon, Geoffrey D.,Al-Dulayymi, Juma R.,Baird, Mark S.,Knobl, Stefan,Roberts, Evan,Minnikin, David E.
, p. 1211 - 1222 (2007/10/03)
(11R,12S)-Lactobacillic acid has been prepared from 2,3-O-isopropylidene-D-glyceraldehyde, in a sequence involving asymmetric cyclopropanation, and from cis-cyclopropane-1,2-dimethanol, using enzymatic desymmetrisation. The key step in the former route wa
The synthesis of a 5-HETE photoaffinity ligand
Saha,Khanapure,Powell,Rokach
, p. 6313 - 6317 (2007/10/03)
The design and synthesis of a photoaffinity ligand 26, targeted at the 5h-dh, was accomplished. The synthesis was effected by two new synthetic routes which focus on the ω-hydroxy 5-HETE derivative 12 as a pivotal synthon. Preliminary results show ligand 26 to be an excellent substrate for the 5h-dh. (C) 2000 Elsevier Science Ltd.
