67563
3,4-Dihydroxy-5-methoxycinnamic acid
≥95.0% (HPLC)
别名:
3-(3,4-Dihydroxy-5-methoxyphenyl)-2-propenoic acid, 3-Methoxycaffeic acid, 5-Hydroxyferulic acid
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关于此项目
经验公式（希尔记法）:
C10H10O5
化学文摘社编号:
分子量:
210.18
UNSPSC Code:
12352106
NACRES:
NA.25
PubChem Substance ID:
MDL number:
Beilstein/REAXYS Number:
2697317
Quality Level
InChI
1S/C10H10O5/c1-15-8-5-6(2-3-9(12)13)4-7(11)10(8)14/h2-5,11,14H,1H3,(H,12,13)/b3-2+
SMILES string
COc1cc(\C=C\C(O)=O)cc(O)c1O
InChI key
YFXWTVLDSKSYLW-NSCUHMNNSA-N
assay
≥95.0% (HPLC)
form
solid
application(s)
metabolomics
vitamins, nutraceuticals, and natural products
Biochem/physiol Actions
Secondary plant metabolite of the phenylpropanoid pathway.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
John M Humphreys et al.
Current opinion in plant biology, 5(3), 224-229 (2002-04-19)
Considerable interest in lignin biosynthesis has been fueled by the many roles that lignin plays in development and in resistance to biotic and abiotic stress, as well as its importance to industry and agriculture. Although the pathway leading to the
Probing the mysteries of lignin biosynthesis: the crystal structure of caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase provides new insights.
Nancy A Eckardt
The Plant cell, 14(6), 1185-1189 (2002-06-27)
K Inoue et al.
Archives of biochemistry and biophysics, 375(1), 175-182 (2000-02-23)
Caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase (COMT, EC 1.2.1.68) catalyzes at least two reactions in lignin biosynthesis. Of its two supposed substrates in the lignin pathway, COMT from most sources methylates 5-hydroxyferulic acid (5HFA) with two to three times higher activity than
I Muzac et al.
Archives of biochemistry and biophysics, 375(2), 385-388 (2000-03-04)
We report that the cDNA clone (Accession No. U70424), previously isolated from Arabidopsis thaliana as encoding a caffeic acid/5-hydroxyferulic acid O-methyltransferase (OMT) (1), has now been overexpressed in Escherichia coli BL21 and its recombinant protein identified as a novel flavonol
R C Bugos et al.
Phytochemistry, 31(5), 1495-1498 (1992-05-01)
Bispecific O-methyltransferase (OMT, EC 2.1.1.68) which catalyses the meta-specific methylation of caffeic acid and 5-hydroxyferulic acid was purified to homogeneity from the developing secondary xylem of aspen (Populus tremuloides). The enzyme was purified by conventional techniques and affinity chromatography on
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