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Quality Level
Assay
99%
form
liquid
refractive index
n20/D 1.426 (lit.)
bp
115 °C (lit.)
density
0.969 g/mL at 25 °C (lit.)
storage temp.
2-8°C
SMILES string
C\C=N\O
InChI
1S/C2H5NO/c1-2-3-4/h2,4H,1H3/b3-2+
InChI key
FZENGILVLUJGJX-NSCUHMNNSA-N
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Related Categories
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Acute Tox. 3 Inhalation - Acute Tox. 4 Oral - Aquatic Chronic 3 - Eye Irrit. 2 - Flam. Liq. 3
WGK
WGK 1
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
危险化学品
Certificates of Analysis (COA)
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The Journal of biological chemistry, 275(43), 33712-33717 (2000-08-03)
Glucosinolates are natural plant products known as flavor compounds, cancer-preventing agents, and biopesticides. We report cloning and characterization of the cytochrome P450 CYP79B2 from Arabidopsis. Heterologous expression of CYP79B2 in Escherichia coli shows that CYP79B2 catalyzes the conversion of tryptophan
Solid phase asymmetric synthesis of isoxazolines.
Journal of combinatorial chemistry, 2(1), 6-7 (2000-04-06)
Chembiochem : a European journal of chemical biology, 7(12), 2004-2009 (2006-09-30)
Phenylacetaldoxime dehydratase from Bacillus sp. OxB-1 (OxdB) contains a heme that acts as the active site for the dehydration reaction of aldoxime. Ferrous heme is the active form, in which the heme is five coordinate with His282 as a proximal
Mutation research, 537(2), 201-208 (2003-06-06)
Acetaldehyde oxime was found to induce more revertants in Salmonella typhimurium strain TA1535 than in TA100 in the absence of S9 metabolic activation. TA100 was originally constructed from TA1535 by the addition of the plasmid pKM101, carrying mucAB which generally
The journal of physical chemistry. B, 116(31), 9396-9408 (2012-07-18)
Aldoxime dehydratase is a heme-containing enzyme that utilizes the ferrous rather than the ferric ion to catalyze the synthesis of nitriles by dehydration of the substrate. We report a theoretical study of this enzyme aimed at elucidating its catalytic mechanism
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