Recommended Products
biological source
synthetic
assay
≥98%
refractive index
n20/D 1.452 (lit.)
bp
110-112 °C/15 mmHg (lit.)
density
1.037 g/mL at 25 °C (lit.)
application(s)
flavors and fragrances
documentation
see Safety & Documentation for available documents
food allergen
no known allergens
organoleptic
sweet
SMILES string
CC1CCCC(=O)O1
InChI
1S/C6H10O2/c1-5-3-2-4-6(7)8-5/h5H,2-4H2,1H3
InChI key
RZTOWFMDBDPERY-UHFFFAOYSA-N
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Storage Class
10 - Combustible liquids
wgk_germany
WGK 2
flash_point_f
224.6 °F
flash_point_c
107 °C
ppe
Eyeshields, Gloves
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Biochemical pharmacology, 66(6), 887-896 (2003-09-10)
Human paraoxonase (PON1) was previously shown to hydrolyze over 30 different lactones (cyclic esters). In the present study purified human PON1 was found to catalyze the reverse reaction (lactonization) of a broad range of hydroxy acids. Hydroxy acid lactonization or
Journal of lipid research, 46(6), 1239-1247 (2005-03-18)
The paraoxonase (PON) gene family in humans has three members, PON1, PON2, and PON3. Their physiological role(s) and natural substrates are uncertain. We developed a baculovirus-mediated expression system, suitable for all three human PONs, and optimized procedures for their purification.
Bioorganic & medicinal chemistry, 16(15), 7504-7509 (2008-06-24)
Paraoxonase1 (PON1) is a HDL bound enzyme and many of the anti-atherogenic properties of HDL are attributed to PON1. The enzyme precise mechanism of protective action and its endogenous substrate remain elusive. PON1 hydrolyzes organophosphates, arylesters and lactones, whereas the
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