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4-Methoxymandelsäure
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About This Item
Lineare Formel:
CH3OC6H4CH(OH)CO2H
CAS-Nummer:
Molekulargewicht:
182.17
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352100
PubChem Substanz-ID:
NACRES:
NA.22
Form:
solid
Assay:
98%
Empfohlene Produkte
Assay
98%
Form
solid
mp (Schmelzpunkt)
108-111 °C (lit.)
SMILES String
COc1ccc(cc1)C(O)C(O)=O
InChI
1S/C9H10O4/c1-13-7-4-2-6(3-5-7)8(10)9(11)12/h2-5,8,10H,1H3,(H,11,12)
InChIKey
ITECRQOOEQWFPE-UHFFFAOYSA-N
Allgemeine Beschreibung
Chiral separation of the enantiomers of 4-methoxymandelic acid has been reported by a new liquid chromatographic method. The mechanism of veratryl alcohol-mediated oxidation of 4-methoxymandelic acid by lignin peroxidase has been studied by kinetic methods.
Lagerklassenschlüssel
13 - Non Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
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M Tien et al.
The Journal of biological chemistry, 272(14), 8912-8917 (1997-04-04)
The mechanism of veratryl alcohol-mediated oxidation of 4-methoxymandelic acid by lignin peroxidase was studied by kinetic methods. For monomethoxylated substrates not directly oxidized by lignin peroxidase, veratryl alcohol has been proposed to act as a redox mediator. Our previous study
P J Teunissen et al.
FEBS letters, 439(3), 219-223 (1998-12-09)
Poly R478, 4-methoxymandelic acid and oxalic acid were oxidized by lignin peroxidase (LiP) in the presence of the fungal metabolite 2-chloro-1,4-dimethoxybenzene (2Cl-14DMB), whereas no oxidation occurred in the absence of 2Cl-14DMB. These substrates clearly inhibited the consumption of 2Cl-14DMB and
L P Candeias et al.
The Journal of biological chemistry, 270(28), 16745-16748 (1995-07-14)
The formation and decay of veratryl alcohol radical cation upon oxidation of veratryl alcohol by thallium (II) ions was studied by pulse radiolysis with spectrophotometric and conductometric detection. In aqueous solution at pH 3 the radical cation decays by a
Radical cation cofactors in lignin peroxidase catalysis.
P J Harvey et al.
Biochemical Society transactions, 23(2), 262-267 (1995-05-01)
K Valli et al.
Biochemistry, 29(37), 8535-8539 (1990-09-18)
Lignin peroxidase (LiP), an extracellular heme enzyme from the lignin-degrading fungus Phanerochaete chrysosporium, catalyzes the H2O2-dependent oxidation of a variety of nonphenolic lignin model compounds. The oxidation of monomethoxylated lignin model compounds, such as anisyl alcohol (AA), and the role
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