87395-84-4Relevant academic research and scientific papers
Probing the active site of rat porphobilinogen synthase using newly developed inhibitors
Li, Nan,Chu, Xiusheng,Liu, Xiaojun,Li, Ding
scheme or table, p. 33 - 40 (2009/05/30)
The structurally related tetrapyrrolic pigments are a group of natural products that participate in many of the fundamental biosynthetic and catabolic processes of living organisms. Porphobilinogen synthase catalyzes a rate-limiting step for the biosyntheses of tetrapyrrolic natural products. In the present study, a variety of new substrate analogs and reaction intermediate analogs were synthesized, which were used as probes for studying the active site of rat porphobilinogen synthase. The compounds 1, 3, 6, 9, 14, 16, and 28 were found to be competitive inhibitors of rat porphobilinogen synthase with inhibition constants ranging from 0.96 to 73.04 mM. Compounds 7, 10, 12, 13, 15, 17, 18, and 26 were found to be irreversible enzyme inhibitors. For irreversible inhibitors, loose-binding inhibitors were found to give stronger inactivation. The amino group and carboxyl group of the analogs were found to be important for their binding to the enzyme. This study increased our understanding of the active site of porphobilinogen synthase.
Studies on the Hydrolysis of Clavulanic Acid
Finn, Malcolm J.,Harris, Michael A.,Hunt, Eric,Zomaya, Iskander I.
, p. 1345 - 1349 (2007/10/02)
1-Amino-4-hydroxybutan-2-one (14) has been identified as one of the major products from the hydrolysis of clavulanic acid in acidic, alkaline, or neutral solution.In alkaline or neutral solution, the amino ketone (14) is converted into other products, including two pyrazines, 2,5-bis(2-hydroxyethyl)pyrazine and 3-ethyl-2,5-bis(2-hydroxyethyl)pyrazine.A rationale for the formation of these products is discussed.
