Formylglycine-generating enzyme (FGE) catalyzes in newly synthesized sulfatases the oxidation of a specific cysteine residue to formylglycine, which is the catalytic residue required for sulfate ester hydrolysis. This post-translational modification occurs in the endoplasmic reticulum (ER), and is an essential
Electric discharges between a pair of carbon electrodes were continued for 50 days in a vessel of 5 liters in volume which initially contained nitrogen at a pressure of 15 cm Hg and 200 ml of water. The pressure in
Proceedings of the National Academy of Sciences of the United States of America, 101(21), 7897-7901 (2004-05-14)
To determine the effectiveness of the ribosome as a catalyst, we compared the rate of uncatalyzed peptide bond formation, by the reaction of the ethylene glycol ester of N-formylglycine with Tris(hydroxymethyl)aminomethane, with the rate of peptidyl transfer by the ribosome.
The journal of physical chemistry. A, 110(28), 8653-8662 (2006-07-14)
Single crystals of the 1:1 complex of the nucleic acid base cytosine and the dipeptide N-formylglycine (C.NFG) have been irradiated at 10 and 273 K to doses of about 70 kGy and studied at temperatures between 10 and 293 K
Journal of enzyme inhibition, 13(5), 369-376 (1998-10-30)
N-formylglycine was developed as a dead-end inhibitor of the succinic semialdehyde dehydrogenase reaction. At 4 mM, it inhibited Aspergillus niger succinic semialdehyde dehydrogenase by 40%. N-formylglycine is a reversible, complete inhibitor; the inhibition is competitive with succinic semialdehyde and uncompetitive
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