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In the complex pathway of histidine biosynthesis, a key branch point linking amino acid and purine biosynthesis is catalyzed by the bifunctional enzyme imidazole glycerol phosphate (IGP) synthase. The first domain of IGP synthase, a triad glutamine amidotransferase, hydrolyzes glutamine to form glutamate and ammonia. Its activity is tightly regulated by the binding of the substrate PRFAR to its partner...
Background: Imidazole glycerol phosphate synthase catalyzes a two-step reaction of histidine biosynthesis at the bifurcation point with the purine de novo pathway. The enzyme is a new example of intermediate channeling by glutamine amidotransferases in which ammonia generated by hydrolysis of glutamine is channeled to a second active site where it acts as a nucleophile. In this case, ammonia reacts...
A rapid and simple HPLC assay has been developed to separate and quantify N-acyl glutamates and the corresponding carboxylic acids of the acyl moiety. This method was specifically developed to assay hydrolytic activity for glutamate carboxypeptidases. Although established assays for specific substrates of such enzymes exist, they may not be amenable for examining the hydrolytic activity of new substrate...
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