00878
(±)-2-Acetoxypropionic acid
≥97.0% (GC)
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About This Item
Productos recomendados
Quality Level
assay
≥97.0% (GC)
refractive index
n20/D 1.423
density
1.176 g/mL at 20 °C (lit.)
SMILES string
CC(OC(C)=O)C(O)=O
InChI
1S/C5H8O4/c1-3(5(7)8)9-4(2)6/h3H,1-2H3,(H,7,8)
InChI key
WTLNOANVTIKPEE-UHFFFAOYSA-N
Categorías relacionadas
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
10 - Combustible liquids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type ABEK (EN14387) respirator filter
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Metabolic engineering, 13(6), 638-647 (2011-08-10)
Diacetyl causes an unwanted buttery off-flavor in lager beer. It is spontaneously generated from α-acetolactate, an intermediate of yeast's valine biosynthesis released during the main beer fermentation. Green lager beer has to undergo a maturation process lasting two to three
Journal of bacteriology, 179(20), 6285-6293 (1997-10-23)
The alpha-acetolactate decarboxylase gene aldB is clustered with the genes for the branched-chain amino acids (BCAA) in Lactococcus lactis subsp. lactis. It can be transcribed with BCAA genes under isoleucine regulation or independently of BCAA synthesis under the control of
Biochimica et biophysica acta, 1245(3), 366-370 (1995-12-14)
Acetolactate nonenzymatically reduced flavins, quinones and nicotinamide coenzymes in a time-dependent manner at physiological pH and moderate temperature. In the presence of excess acetolactate, the reduction of FAD and NAD+ followed pseudo-first-order kinetics. The rate of reduction was proportional to
Biochemistry, 40(25), 7369-7381 (2001-06-20)
Yeast pyruvate decarboxylase (YPDC), in addition to forming its metabolic product acetaldehyde, can also carry out carboligase reactions in which the central enamine intermediate reacts with acetaldehyde or pyruvate (instead of the usual proton electrophile), resulting in the formation of
Analytical biochemistry, 342(1), 126-133 (2005-06-17)
Acetohydroxy acid synthase (AHAS) and related enzymes catalyze the production of chiral compounds [(S)-acetolactate, (S)-acetohydroxybutyrate, or (R)-phenylacetylcarbinol] from achiral substrates (pyruvate, 2-ketobutyrate, or benzaldehyde). The common methods for the determination of AHAS activity have shortcomings. The colorimetric method for detection
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