SMILES string
C[C@H](OC(C)=O)C(O)=O
assay
95%
optical activity
[α]20/D −51°, c = 7 in chloroform
impurities
<5% acetic acid
refractive index
n20/D 1.422 (lit.)
bp
115-117 °C/2 mmHg (lit.)
density
1.162 g/mL at 25 °C (lit.)
存储类别
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
235.4 °F - closed cup
flash_point_c
113 °C - closed cup
法规信息
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Michael Vinogradov et al.
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
Ahmet Baykal et al.
Bioorganic chemistry, 34(6), 380-393 (2006-11-07)
In addition to the decarboxylation of 2-oxo acids, thiamin diphosphate (ThDP)-dependent decarboxylases/dehydrogenases can also carry out so-called carboligation reactions, where the central ThDP-bound enamine intermediate reacts with electrophilic substrates. For example, the enzyme yeast pyruvate decarboxylase (YPDC, from Saccharomyces cerevisiae)
C T Duong et al.
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
N Goupil-Feuillerat et al.
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
H S Park et al.
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
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