Kondo, Hiroki; Uno, Shingo; Moriuchi, Fumio; Sunamoto, Junzo; Ogushi, Susumu; Tsuru, Daisuke published the artcile< Synthesis and enzymatic carboxylation of a biotin-containing peptide representing the coenzyme binding site of E. coli acetyl-CoA carboxylase>, Electric Literature of 112-63-0, the main research area is acetyl CoA carboxylase biotin binding site; peptide biotin acetyl CoA carboxylase.
A biotin-containing pentapeptide, Boc-Glu-Ala-Met-Bct-Met (I) (where Boc = tert-butoxycarbonyl and Bct = N’-biotinyl-L-lysine), that corresponds to the coenzyme-binding site of Escherichia coli acetyl-CoA carboxylase (II) was prepared I, as well as free biotin, served as substrate for the carboxylation reaction catalyzed by the biotin carboxylase subunit dimer of E. coli II. The Km and Vmax values for I were 18 mM and 2.8 μM min-1, resp. The corresponding values for biotin were 214 mM and 28 μM min-1. Thus, the overall reactivity (Vmax/Km) of I exceeded that of biotin by 20%.
Bulletin of the Chemical Society of Japan published new progress about Escherichia coli. 112-63-0 belongs to class esters-buliding-blocks, and the molecular formula is C19H34O2, Electric Literature of 112-63-0.
Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics