Pseudomonas aeruginosa porphobilinogen synthase assembly state regulators: hit discovery and initial SAR studies was written by Reitz, Allen B.;Ramirez, Ursula D.;Stith, Linda;Du, Yanming;Smith, Garry R.;Jaffe, Eileen K.. And the article was included in ARKIVOC (Gainesville, FL, United States) in 2010.Reference of 74704-39-5 The following contents are mentioned in the article:
Porphobilinogen synthase (PBGS) catalyzes the first common step in the biosynthesis of the essential heme, chlorophyll and vitamin B12 heme pigments. PBGS activity is regulated by assembly state, with certain oligomers exhibiting biol. activity and others either partially or completely inactive, affording an innovative means of allosteric drug action. Pseudomonas aeruginosa PBGS is functionally active as an octamer, and inactive as a dimer. We have identified a series of compounds that stabilize the inactive P. aeruginosa dimer by a computational prescreen followed by native PAGE gel mobility shift anal. From those results, we have prepared related thiadiazoles and evaluated their ability to regulate P. aeruginosa PBGS assembly state. This study involved multiple reactions and reactants, such as 4-(Bromomethyl)-2-methylthiazole (cas: 74704-39-5Reference of 74704-39-5).
4-(Bromomethyl)-2-methylthiazole (cas: 74704-39-5) belongs to thiazole derivatives. Thiazoles in peptides or their ability to bind proteins, DNA and RNA has led to many synthetic studies and new applications. The pyridine-type nitrogen in the thiazole ring deactivates the ring for electrophilic substitution reactions, which is further reduced in acid due to protonation of the thiazole ring.Reference of 74704-39-5
Referemce:
Thiazole | C3H3NS – PubChem,
Thiazole | chemical compound | Britannica