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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.
包装
Bottomless glass bottle. Contents are inside inserted fused cone.
WGK
WGK 3
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Metabolic profiling by ion mobility mass spectrometry (IMMS).
Dwivedi, P., et al.
Metabolomics, 4, 63-80 (2008)
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
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
Enzymic synthesis of 4-methyl- and 4-ethyl-L-glutamic acids .
Echalier, F., et al.
The Journal of Organic Chemistry, 58, 2747-2750 (1993)
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
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