96599
DL-4-Hydroxy-2-ketoglutaric acid lithium salt
≥90.0% (TLC)
别名:
4-Hydroxy-2-oxoglutaric acid lithium salt, DL-KHG Li
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关于此项目
经验公式（希尔记法）:
C5H6O6 · xLi+
化学文摘社编号:
分子量:
162.10 (free acid basis)
MDL number:
UNSPSC Code:
12352106
NACRES:
NA.28
Beilstein/REAXYS Number:
1780096
SMILES string
OC(CC(=O)C(=O)O)C(=O)O
InChI
1S/C5H6O6/c6-2(4(8)9)1-3(7)5(10)11/h2,6H,1H2,(H,8,9)(H,10,11)
InChI key
WXSKVKPSMAHCSG-UHFFFAOYSA-N
assay
≥90.0% (TLC)
form
solid
impurities
≤15.0% water, 3.9-8.4% lithium (anhydrous basis)
storage temp.
−20°C
Quality Level
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Biochem/physiol Actions
DL-4-Hydroxy-2-ketoglutaric acid (DL-KHG) is an enzyme substrate for GOT (glutamic oxalacetic aminotransferase) and 2-Keto-4-hydroxyglutarate aldolase, which catalyzes the reversible cleavage of 2-keto-4-hydroxyglutarate yielding pyruvate plus glyoxylate; DL-KHG has been used in mass spectrometry for the rapid analysis of negatively charged water-soluble cellular metabolites.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Metabolic profiling by ion mobility mass spectrometry (IMMS).
Dwivedi, P., et al.
Metabolomics, 4, 63-80 (2008)
T S Taha et al.
Biochemical and biophysical research communications, 200(1), 459-466 (1994-04-15)
2-keto-3-deoxy-6-phosphogluconate aldolase (E.C. 4.1.2.14) has been purified in two chromatographic steps to 99% purity in 73% overall yield from Azotobacter vinelandii. The pure enzyme is a 70 kD trimeric Class I aldolase, inhibitable by bromopyruvate or pyruvate plus sodium borohydride
Enzymic synthesis of 4-methyl- and 4-ethyl-L-glutamic acids .
Echalier, F., et al.
The Journal of Organic Chemistry, 58, 2747-2750 (1993)
H C Winter et al.
Biochimica et biophysica acta, 749(1), 52-61 (1983-11-28)
Exposure of Escherichia coli 2-oxo-4-hydroxyglutarate aldolase (4-hydroxy-2-oxoglutarate glyoxylate-lyase, EC 4.1.3.16) (molecular weight = 63 000) to phosphoric acid at pH 1.6 for 10 min at 4 degrees C causes 95% or greater inactivation. No significant effect on the rate or
S C Gupta et al.
The Journal of biological chemistry, 259(16), 10012-10019 (1984-08-25)
The alpha-ketoglutarate dehydrogenase complex of either pig heart or Escherichia coli catalyzes a NAD- and CoASH-dependent oxidation of 2-keto-4-hydroxyglutarate which is stereoselective toward the L-isomer of this hydroxyketo acid. L-Malyl-CoA is the product of the reaction; the evidence includes observing
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