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Key Documents

12271

Sigma-Aldrich

2-Keto-3-deoxy-D-gluconic acid lithium salt

≥95% (TLC)

同義詞:

3-Deoxy-D-erythro-2-hexulosonic acid lithium salt, KDG, Lithium 2-keto-3-deoxy-D-gluconate

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About This Item

經驗公式(希爾表示法):
C6H10O6 · xLi+
CAS號碼:
分子量::
178.14 (free acid basis)
分類程式碼代碼:
12352204
NACRES:
NA.32

化驗

≥95% (TLC)

形狀

powder or crystals

儲存溫度

−20°C

InChI

1S/C6H10O6/c7-2-5(10)3(8)1-4(9)6(11)12/h3,5,7-8,10H,1-2H2,(H,11,12)/t3-,5+/m0/s1

InChI 密鑰

WPAMZTWLKIDIOP-WVZVXSGGSA-N

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生化/生理作用

Metabolite in the pentose phosphate pathway, which generates NADPH and pentoses; KDG is an intermediate in the metabolism of glucose and gluconic acid in some pseudomonas strains, of uronic acids in E. coli, and also an important metabolite in the degradation of polygalacturonates in Erwinia chrysanthemi.

包裝

Bottomless glass bottle. Contents are inside inserted fused cone.

注意

Hygroscopic.

分析證明 (COA)

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A new pathway of uronic acid metabolism.
A ASHWELL et al.
Biochimica et biophysica acta, 30(1), 186-187 (1958-10-01)
Uronic acid metabolism in bacteria. IV. Purification and properties of 2-keto-3-deoxy-D-gluconokinase in Escherichia coli.
M A CYNKIN et al.
The Journal of biological chemistry, 235, 1576-1579 (1960-06-01)
Glucose and gluconic acid oxidation of Pseudomonas saccharophila.
N ENTNER et al.
The Journal of biological chemistry, 196(2), 853-862 (1952-05-01)
Carbohydrate metabolism by Pseudomonas fluorescens. III. Purification and properties of a 6-phosphogluconate dehydrase.
R KOVACHEVICH et al.
The Journal of biological chemistry, 213(2), 745-756 (1955-04-01)
Viatcheslav Zaitsev et al.
Biochemistry, 57(26), 3797-3806 (2018-05-31)
The thermoacidophilic archaea Picrophilus torridus and Sulfolobus solfataricus catabolize glucose via a nonphosphorylative Entner-Doudoroff pathway and a branched Entner-Doudoroff pathway, respectively. Key enzymes for these Entner-Doudoroff pathways are the aldolases, 2-keto-3-deoxygluconate aldolase (KDG-aldolase) and 2-keto-3-deoxy-6-phosphogluconate aldolase [KD(P)G-aldolase]. KDG-aldolase from P.

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