Disease relevance of Ethoxyformic anhydride

• Chemical modification of Escherichia coli alkaline phosphatase using the group-specific reagent, ethoxyformic anhydride, has demonstrated that 3 histidyl residues/subunit are modified with a concomitant loss of enzyme activity [1].
• The number and role of histidine residues in the active site of extracellular guanyloribonuclease Sa produced by Streptomyces aureofaciens (RNAase Sa) were studied via chemical modification by ethoxyformic anhydride by means of circular dichroism measurements [2].

High impact information on Ethoxyformic anhydride

• The fourth derivative (EF actin), in which histidine-40 is labeled with ethoxyformic anhydride, binds to membranes with reduced affinity [3].
• His99 modification at the hh-dimer interface by ethoxyformic anhydride abolished ANP binding [4].
• Diferric human serum transferrin was chemically modified to various extents using ethoxyformic anhydride, a reagent for histidines [5].
• The immobilized dimeric alkaline phosphatase was inactivated with ethoxyformic anhydride at a rate similar to that of the soluble enzyme, demonstrating that immobilization did not significantly alter the chemical environment of the Zn2+ binding site [1].
• Reaction of the histidines of prolactin with ethoxyformic anhydride. A binding site modification [6].

Biological context of Ethoxyformic anhydride

• Addition of regulatory subunit or Mg2+-ATP to the isolated catalytic subunit also prevents ethoxyformic anhydride inactivation [7].
• Both diphenileneiodonium and ethoxyformic anhydride (inhibitors for respiratory components located upstream of the respiratory chain) inhibited the enhancement by rotenone and piericidin A.In contrast, in reverse electron transfer driven by ATP, both diphenileneiodonium and ethoxyformic anhydride enhanced the superoxide production [8].
• The activity of the fragment towards p-nitrophenyl acetate hydrolysis is inhibited after ethoxyformic anhydride reaction as in the case of lipase [9].
• Strong binding to egg PC was observed, which was not dependent on the presence of calcium ion (essential for catalysis); PLA inhibited by acylation of up to four lysine residues per mole of monomeric enzyme with ethoxyformic anhydride was equally strongly adsorbed, indicating that lipid binding is not dependent on catalytic activity [10].

Anatomical context of Ethoxyformic anhydride

• The rotenone-stimulated NADH-supported superoxide production of the heart and nonsynaptic brain mammalian submitochondrial particles was inhibited both by p-chloromercuribenzoate and by ethoxyformic anhydride [11].
• Purified and membrane-bound succinate dehydrogenase (SDH) from bovine heart mitochondria was inhibited by the histidine-modifying reagents ethoxyformic anhydride (EFA) and Rose Bengal in the presence of light [12].

Associations of Ethoxyformic anhydride with other chemical compounds

• A methodology is described for purification of histidyl peptides based on the changes in hydrophobicity induced by the specific and reversible modification of histidine residues by ethoxyformic anhydride [13].
• Modification of bovine heart succinate dehydrogenase with ethoxyformic anhydride and rose bengal: evidence for essential histidyl residues protectable by substrates [12].
• Exposure of calf uterine estradiol-receptor complexes to diethylpyrocarbonate (ethoxyformic anhydride) at pH 6.3-6.5 results in a decrease in the ability of the receptor to bind to oligodeoxyribonucleotides [14].
• At least four histidine residues were concomitantly modified by ethoxyformic anhydride at pH 6; both the GSSG reductase and the transhydrogenase activities were inhibited to the same extent [15].
• Upon treatment with DFP as well as with ethoxyformic anhydride, the enzyme remains able to bind to the model interface formed by siliconized glass-beads with almost the same efficiency (Kd between 4.1 and 7.4.10(-8) M) than the native bile-salt-stimulated lipase (Kd = 6.3.10(-8) M) [16].

Gene context of Ethoxyformic anhydride

• Modification of human growth hormone and human placental lactogen with ethoxyformic anhydride resulted in a loss of the ability of these lactogenic hormones to bind to the prolactin receptor [6].
• The seven histidines of bovine prolactin were modified with ethoxyformic anhydride and two classes of reactivity were apparent: 5 histidines were in the more reactive class (k = 0.097 min-1) and 2 histidines were less reactive (k = 0.011 min-1) [6].
• At pH 4.5, 2'-adenylate and 2'-guanylate protected RNase U2 from inactivation by ethoxyformic anhydride [17].
• Mechanism of pigeon liver malic enzyme modification of histidyl residues by ethoxyformic anhydride [18].

Analytical, diagnostic and therapeutic context of Ethoxyformic anhydride

• The catalytically inactive, immobilized monomer of alkaline phosphatase was modified more rapidly with ethoxyformic anhydride, demonstrated by the loss of its ability to form functionally active enzyme upon titration with nascent soluble subunits [1].

References