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95440

Sigma-Aldrich

2-Ethyl-5-phenylisoxazolium-3′-sulfonate

purum, ≥97.0% (T)

Sinônimo(s):

Woodwards reagent K

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About This Item

Fórmula empírica (Notação de Hill):
C11H11NO4S
Número CAS:
4156-16-5
Peso molecular:
253.27
Beilstein:
4149224
Número CE:
223-988-7
Número MDL:
MFCD00012128
Código UNSPSC:
12352005
ID de substância PubChem:
329770460

grau

purum

Ensaio

≥97.0% (T)

pf

216-219 °C (dec.)

cadeia de caracteres SMILES

CC[n+]1ccc(o1)-c2cccc(c2)S([O-])(=O)=O

InChI

1S/C11H11NO4S/c1-2-12-7-6-11(16-12)9-4-3-5-10(8-9)17(13,14)15/h3-8H,2H2,1H3

chave InChI

MWOOKDULMBMMPN-UHFFFAOYSA-N

Outras notas

Modification of carboxylic groups in enzymes; Coupling reagent for peptide synthesis

substituído por

Nº do produto
Descrição
Preços

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

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M S Saini et al.
Biochimica et biophysica acta, 568(2), 370-376 (1979-06-06)
Treatment of homogenous human prostatic acid phosphatase (orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2) with low concentrations of Woodward's reagent K (N-ethyl-5-phenylisoxazolium-3'-sulfonate) leads to a rapid loss of enzymic activity. The rate of inactivation of the enzyme is reduced in the
V.L. Boyd et al.
Tetrahedron Letters, 31, 3849-3849 (1990)
A A Komissarov et al.
The Journal of biological chemistry, 270(17), 10050-10055 (1995-04-28)
Woodward's reagent K (WRK) completely inactivated Escherichia coli uridine phosphorylase by reversible binding in the active site (Ki = 0.07 mM) with subsequent modification of a carboxyl (k2 = 1.2 min-1). Neither substrate alone protected uridine phosphorylase from inactivation. The
S R Rao et al.
Indian journal of biochemistry & biophysics, 34(3), 253-258 (1997-06-01)
Maize leaf NADP-malic enzyme was rapidly inactivated by micromolar concentrations of Woodward's reagent K (WRK). The inactivation followed pseudo-first order reaction kinetics. The order of reaction with respect to WRK was 1, suggesting that inactivation was a consequence of the
G Feller et al.
The Journal of biological chemistry, 271(39), 23836-23841 (1996-09-27)
Chloride is the allosteric effector of vertebrate pancreatic and salivary alpha-amylases and of the bacterial alpha-amylase from Alteromonas haloplanctis. Activation experiments of A. haloplanctis alpha-amylase by several monovalent anions show that a negative charge, not restricted to that of Cl-
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