Enzymatic synthesis of 4-OH-benzoic acid from phenol CO2: The first example of a biotechnological application of a carboxylase enzyme
4-OH benzoic acid has been synthesized from phenol CO2 at room temperature sub-atmospheric pressure of CO2 with 100%ivity, using a Carboxylase enzyme. A cheap, fast easy method fthe phosphorylation of phenol has been also developed. This represents the first biotechnological application of a Carboxylase enzyme.
Inhibition of serine β-lactamases by acyl phosph(on)ates: A new source of inert acyl [phosphyl] enzymes
Acyl phosph(on)ates are shown to inhibit serine β-lactamases provide a new source of relatively stable complexes. Thus, benzoyl phenyl phosphate, benzoyl phenylphosphonate, dibenzoyl phosphate react with the class C β-lactamase of Enterobacter cloacae P99 at micromolar concentrations to form an acyl enzyme of half-life about 40 s. The phosphonate reacts further more slowly to produce a much more inert complex. Dibenzoyl phosphate reacts with the class A TEM β-lactamase to from an acyl enzyme of half-life about 8 s, more slowly, reaching completion after an average of about 80 turnovers, a more inert complex, of half-life about 2 h. The acyl phosphonates thus represent a new starting point fthe design of β- lactamase inhibitors perhaps of antibacterial agents.
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