Metabolism of phosphoramidates II. Further studies on the Escherichia coli phosphoramidate phosphoryl transfer enzyme

The HS:1 serostrain ofCampylobacter jejunihas a complex teichoic acid‐like capsular polysaccharide with nonstoichiometric fructofuranose branches andO‐methyl phosphoramidate groups

“…Phosphoramidate structures are quite rare in nature and have not, to our knowledge, been shown to exist on CPS for any other bacterium and therefore appear to be unique to C. jejuni. Previous work examining synthetic phosphoramidate molecules have shown that they are high energy, labile structures with large standard free energies of hydrolysis and greater phospho donor potential than ATP [35–37]. Although very little is known about their biological role in vivo , because of their reactive nature and high phosphodonor capabilities, phosphoramidates are thought to interact nonspecifically with accessible amino acids of proteins [38].…”

Evaluation of Natural and Synthetic Phosphate Donors for the Improved Enzymatic Synthesis of Phosphate Monoesters

“…Organic P‐donors have been used with phosphatases in the hydrolysis‐ and transphosphorylation‐mode, however, product isolation has scarcely been reported 27,44,45. Aryl phosphates (e. g. phenyl phosphate, p ‐nitrophenyl phosphate, phenolphthalein phosphate) and various metabolites (e. g. nucleoside phosphates, sugar‐phosphates) have been commonly used in biochemical characterization of novel enzymes due to their availability and features allowing facile spectrophotometric or NMR analysis.…”

Phosphoramidates. V. Probable identity of rat liver microsomal glucose 6-phosphatase, phosphoramidase, and phosphoramidate-hexose phosphotransferase

“…A comparison of these two enzyme activities with that of glucose 6-phosphatase revealed that all three activities behaved alike under a variety of conditions. Evidence suggesting the involvement of a single enzyme catalyzing It was reported previously that Escherichia coli extract had an enzyme that in addition to hydrolyzing phosphoramidate also catalyzed phosphotransferase reactions with relatively low concentrations of glucose as acceptor (Fujimoto and Smith, 1962). Subsequently Holzer et al (1966) found that the microsomal fraction of liver and kidney also possessed similar enzymatic activities and suggested that these enzymatic activities were unrelated to the microsomal glucose 6-phosphatase activity which had been reported to catalyze pyrophosphatase and pyrophosphate glucose phosphotransferase reactions also (Stetten and Taft, 1964; Nordlie and .…”