N1895
4-Nitrophenyl α-D-xylopyranoside
α-xylosidase substrate, ≥99% (HPLC), powder
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Product Name
4-Nitrophenyl α-D-xylopyranoside, α-xylosidase substrate
Quality Level
Assay
≥99% (HPLC)
form
powder
solubility
methanol: soluble 20 mg/mL, clear, colorless to faintly yellow
storage temp.
−20°C
SMILES string
OC1COC(Oc2ccc(cc2)N(=O)=O)C(O)C1O
InChI
1S/C11H13NO7/c13-8-5-18-11(10(15)9(8)14)19-7-3-1-6(2-4-7)12(16)17/h1-4,8-11,13-15H,5H2
InChI key
MLJYKRYCCUGBBV-UHFFFAOYSA-N
Substrates
Chromogenic substrate for α-xylosidase
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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The variation of kinetic parameters of beta-xylosidase from Trichoderma reesei QM 9414 with pH was used to elucidate the chemical mechanism of the p-nitrophenyl beta-D-xylopyranoside hydrolysis. The pH-dependence of V and V/K(m) showed that a group on the enzyme with
Carbohydrate research, 339(7), 1353-1360 (2004-04-29)
Di-O-acetates and mono-O-acetates of 4-nitrophenyl beta-D-xylopyranoside were prepared by use of lipase PS-30. Polarity of organic solvents and reaction time affected the regioselectivity of the di-O-acetylation as well as the yields of monoacetates. The kinetics of acetyl groups migration in
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Positional specificity of NodB-like domain of a multidomain xylanase U from Clostridium thermocellum (CtAxe) was investigated. Of three monoacetates of 4-nitrophenyl beta-d-xylopyranoside the acetylxylan esterase domain showed a clear preference for the 2-acetate. Moreover, the enzyme was significantly activated by
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