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N7251

Sigma-Aldrich

4-Nitrocatechol sulfate dipotassium salt

crystalline

Synonym(s):

2-Hydroxy-5-nitrophenyl sulfate, 2-Hydroxy-5-nitrophenyl sulfate dipotassium salt monohydrate, p-Nitrocatechol sulfate dipotassium salt

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About This Item

Linear Formula:
C6H3NO7SK2
CAS Number:
14528-64-4
Molecular Weight:
311.35
Beilstein:
3805018
EC Number:
238-550-0
MDL number:
MFCD00007465
UNSPSC Code:
12352200
PubChem Substance ID:
24897816
NACRES:
NA.77

form

crystalline

color

yellow

storage temp.

−20°C

SMILES string

[K+].[K+].[O-]c1ccc(cc1OS([O-])(=O)=O)[N+]([O-])=O

InChI

1S/C6H5NO7S.2K/c8-5-2-1-4(7(9)10)3-6(5)14-15(11,12)13;;/h1-3,8H,(H,11,12,13);;/q;2*+1/p-2

InChI key

CKWWBDCAYRJAJB-UHFFFAOYSA-L

General description

4-Nitrocatechol sulfate is an aromatic sulfate.

Application

4-Nitrocatechol sulfate dipotassium salt has been used as a substrate in mucopolysaccharidoses VI (MPS VI) analysis. It has also been used to measure the activity of glycosaminoglycan (GAG)-degrading enzymes-arylsulfatase B, and exoglycosidases.

Substrates

Chromogenic sulfatase substrate.

Pictograms

Exclamation mark
GHS07

Signal Word

Warning

Hazard Statements

H315,H319,H335

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

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

Certificates of Analysis (COA)

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Mazdak Khajehpour et al.
Biochemistry, 46(14), 4370-4378 (2007-03-14)
The Yersinia protein tyrosine phosphatase (YopH) contains a loop of ten amino acids (the WPD loop) that covers the entrance of the active site of the enzyme during substrate binding. In this work the substrate mimicking competitive inhibitor p-nitrocatechol sulfate
M Recksiek et al.
The Journal of biological chemistry, 273(11), 6096-6103 (1998-04-16)
Sulfatases contain an active site formylglycine residue that is generated by post-translational modification. Crystal structures of two lysosomal sulfatases revealed significant similarity to the catalytic site of alkaline phosphatase containing a serine at the position of formylglycine. To elucidate the
C O'Fagain et al.
The Biochemical journal, 201(2), 345-352 (1982-02-01)
A simple model is described to account for the anomalous time course of arylsulphatase A. In the case of the ox liver and human placental enzymes the enzyme-nitrocatechol sulphate complex can, in addition to forming products, slowly break down to
D B Thompson et al.
Experientia, 42(2), 150-151 (1986-02-15)
Rodent and bovine arylsulfatase B hydrolyze 4-methylumbelliferyl sulfate (4MUS) 10- to 30-fold more efficiently than arylsulfatase A. Therefore, 4MUS grossly underestimates arylsulfatase A activity in the presence of excess arylsulfatase B.
Camila M Adade et al.
Micron (Oxford, England : 1993), 38(3), 252-256 (2006-07-25)
Lysosomes of trypanosomatid protozoa are poorly known. In this work we have cytochemically detected the lysosomal enzyme aryl sulphatase in the trypanosomatids Trypanosoma cruzi and Crithidia fasciculata, by using p-nitrocatecholsulphate as substrate. Positive reaction was located exclusively inside membrane-bound cytoplasmic
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