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方案
≥85.0% (HPLC)
表单
solution
旋光性
[α]/D -2.5±1.5°, 24 hr, c = 2 in H2O
浓度
1 M in water
颜色
colorless to green-yellow
SMILES字符串
O=C(CO)[C@H](O)CO
InChI
1S/C4H8O4/c5-1-3(7)4(8)2-6/h3,5-7H,1-2H2/t3-/m1/s1
InChI key
UQPHVQVXLPRNCX-GSVOUGTGSA-N
生化/生理作用
Metabolite of the erythritol and D-tetrose metabolism.
其他说明
To gain a comprehensive understanding of our extensive range of Monosaccharides for your research, we encourage you to visit our Carbohydrates Category page.
储存分类代码
10 - Combustible liquids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
监管及禁止进口产品
Studies on D-tetrose metabolism. IV. Purification and some properties of D-erythrulose reductase from beef liver.
K Uehara et al.
Journal of biochemistry, 75(2), 333-345 (1974-02-01)
Wayoon Poonperm et al.
Bioscience, biotechnology, and biochemistry, 72(1), 231-235 (2008-01-08)
The conversion specificity of Bacillus pallidus Y25 for polyols, including elusive rare sugar alcohols, was investigated. B. pallidus cells showed transformation potential for several rare polyols, including allitol, L-mannitol, D/L-talitol, and D-iditol, and converted them to their corresponding ketoses. This
J F Sperry et al.
Journal of bacteriology, 121(2), 619-630 (1975-02-01)
Cell extracts of Brucella abortus (British 19) catabolized erythritol through a series of phosphorylated intermediates to dihydroxyacetonephosphate and CO-2. Cell extracts required adenosine 5'-triphosphate (ATP), nicotinamide adenine dinucleotide (NAD), Mg2+, inorganic orthophosphate, and reduced glutathione for activity. The first reaction
Jiangang Yang et al.
Biotechnology and bioengineering, 112(1), 168-180 (2014-07-26)
Rare sugars have various known biological functions and potential for applications in pharmaceutical, cosmetics, and food industries. Here we designed and constructed a recombination pathway in Corynebacterium glutamicum, in which dihydroxyacetone phosphate (DHAP), an intermediate of the glycolytic pathway, and
K Uehara et al.
Journal of biochemistry, 87(1), 47-55 (1980-01-01)
D-Erythrulose reductase from chicken liver has been purified to homogeneity as judged by acrylamide gel electrophoresis and ultracentrifugation. The overall purification of the enzyme was 164-fold from a crude extract. The enzyme was crystallized from ammonium sulfate solution at pH
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