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Assay
≥98.0%
form
solid
reaction suitability
reaction type: solution phase peptide synthesis
mp
149-151 °C
application(s)
peptide synthesis
storage temp.
2-8°C
SMILES string
OC(=O)CNC=O
InChI
1S/C3H5NO3/c5-2-4-1-3(6)7/h2H,1H2,(H,4,5)(H,6,7)
InChI key
UGJBHEZMOKVTIM-UHFFFAOYSA-N
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Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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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
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
The Journal of biological chemistry, 283(29), 20117-20125 (2008-04-09)
Type I sulfatases require an unusual co- or post-translational modification for their activity in hydrolyzing sulfate esters. In eukaryotic sulfatases, an active site cysteine residue is oxidized to the aldehyde-containing C(alpha)-formylglycine residue by the formylglycine-generating enzyme (FGE). The machinery responsible
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.
Journal of molecular biology, 384(1), 120-136 (2008-09-17)
The alkaline phosphatase superfamily comprises a large number of hydrolytic metalloenzymes such as phosphatases and sulfatases. We have characterised a new member of this superfamily, a phosphonate monoester hydrolase/phosphodiesterase from Rhizobium leguminosarum (R/PMH) both structurally and kinetically. The 1.42 A
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