73572
L-(−)-甘油醛
≥90% (HPLC)
别名:
(2S)-2,3-Dihydroxypropanal
质量水平
方案
≥90% (HPLC)
旋光性
[α]/D -11.0±3.0°, c = 2 in H2O (after 24 h)
溶解性
water: soluble 30 g/L at 18 °C
储存温度
2-8°C
SMILES字符串
OC[C@H](O)C=O
InChI
1S/C3H6O3/c4-1-3(6)2-5/h1,3,5-6H,2H2/t3-/m1/s1
InChI key
MNQZXJOMYWMBOU-GSVOUGTGSA-N
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应用
- L-甘油醛通过代谢和信号传导的多模态机制抑制成神经细胞瘤细胞生长。: 这项研究强调了L-甘油醛对成神经细胞瘤细胞生长的抑制作用，揭示了其通过代谢和细胞信号传导的多种途径产生的影响（Forbes M et al., 2024）。
生化/生理作用
L-(-)-甘油醛是碳水化合物代谢中的一种重要中间体。
包装
无底玻璃瓶。内含物在插入的融合锥体内。
储存分类代码
10 - Combustible liquids
WGK
WGK 3
闪点(°F)
233.6 °F - closed cup
闪点(°C)
112 °C - closed cup
David A Korasick et al.
Journal of molecular biology, 431(3), 576-592 (2018-12-24)
Heterokonts, Alveolata protists, green algae from Charophyta and Chlorophyta divisions, and all Embryophyta plants possess an aldehyde dehydrogenase (ALDH) gene named ALDH12. Here, we provide a biochemical characterization of two ALDH12 family members from the lower plant Physcomitrella patens and
Nina Richter et al.
Chembiochem : a European journal of chemical biology, 10(11), 1888-1896 (2009-07-07)
The acetic acid bacterium Gluconobacter oxydans has a high potential for oxidoreductases with a variety of different catalytic abilities. One putative oxidoreductase gene codes for an enzyme with a high similarity to the NADP+-dependent glycerol dehydrogenase (GlyDH) from Hypocrea jecorina.
Nina Richter et al.
Biotechnology and bioengineering, 106(4), 541-552 (2010-03-04)
A whole-cell catalyst using Escherichia coli BL21(DE3) as a host, co-expressing glycerol dehydrogenase (GlyDH) from Gluconobacter oxydans and glucose dehydrogenase (GDH) from Bacillus subtilis for cofactor regeneration, has been successfully constructed and used for the reduction of aliphatic aldehydes, such
Cancer biomarker AKR1B10 and carbonyl metabolism.
Balendiran, G. K., et al.
Chemistry & Biology, 178, 134-137 (2009)
Zhou Chen et al.
Enzyme and microbial technology, 133, 109456-109456 (2019-12-26)
Dihydroxyacetone phosphate (DHAP)-dependent aldolases demonstrate important values in the production of rare ketoses due to their unique stereoselectivities. As a specific example, we developed an efficient Escherichia coli whole-cell biocatalytic cascade system in which rare ketoses were produced from abundant
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