N2881
4-Nitrophenyl phenylphosphonate
adenosine receptor agonist, 5′-Nucleotide Phosphodiesterase substrate
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About This Item
Empirical Formula (Hill Notation):
C12H10NO5P
CAS Number:
Molecular Weight:
279.19
NACRES:
NA.32
PubChem Substance ID:
UNSPSC Code:
12352204
MDL number:
InChI
1S/C12H10NO5P/c14-13(15)10-6-8-11(9-7-10)18-19(16,17)12-4-2-1-3-5-12/h1-9H,(H,16,17)
SMILES string
OP(=O)(Oc1ccc(cc1)N(=O)=O)c2ccccc2
InChI key
NRGZTHQFAQCJCQ-UHFFFAOYSA-N
assay
≥98% (TLC)
form
powder
solubility
acetone: 50 mg/mL, clear, faintly yellow
storage temp.
−20°C
Quality Level
General description
5′-Nucleotide Phosphodiesterase substrate
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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M Labadie et al.
Biochimie, 61(9), 1091-1094 (1979-01-01)
A "Batch" microcalorimeter is used at 30 degrees C for the study of the hydrolysis of 4-nitro-phenylphenylphosphonate with a calf-intestinal phosphonate esterase, in a tris buffer, pH 8. The yield of enzymatic hydrolysis is estimated by spectrophotometric determination of the
H J Deussen et al.
Bioorganic & medicinal chemistry, 8(3), 507-513 (2000-03-25)
A bifunctional activity label (8) for directed molecular evolution of lipolytic enzymes has been designed and synthesized. The structure is composed of a 4-nitrophenyl activated phosphonate, that is, a suicide substrate of lipases/esterases, connected to a biotin moiety through a
Hydrolysis of a phosphonate ester catalyzed by an enzyme from Dictyostelium discoideum.
E F Rossomando et al.
Archives of biochemistry and biophysics, 197(1), 364-366 (1979-10-01)
D S Tawfik et al.
Analytical biochemistry, 202(1), 35-39 (1992-04-01)
Several laboratories have now shown that monoclonal antibodies having enzyme-like properties can be generated. The generation of catalytic antibodies makes use of the same basic procedures that have been used for the generation of binding monoclonal antibodies, yet the process
O A Moe et al.
The Journal of biological chemistry, 258(11), 6941-6946 (1983-06-10)
Extensive kinetic studies of bovine intestinal 5'-nucleotide phosphodiesterase as a function of pH have confirmed and amplified the catalytic mechanism previously proposed on the basis of isolation of a covalent phosphorylated intermediate (Landt, M., and Butler, L.G. (1978) Biochemistry 17
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