37442
二羟丙酮磷酸盐 锂盐
≥95.0% (TLC)
别名:
1-羟基-3-(膦酰氧基)-2-丙酮 锂盐, DHAP, 磷酸甘油酮 锂盐
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关于此项目
经验公式（希尔记法）:
C3H7O6P · xLi+
化学文摘社编号:
分子量:
170.06 (free acid basis)
NACRES:
NA.32
PubChem Substance ID:
UNSPSC Code:
12352204
MDL number:
产品名称
二羟丙酮磷酸盐 锂盐, ≥95.0% (TLC)
InChI
1S/C3H7O6P/c4-1-3(5)2-9-10(6,7)8/h4H,1-2H2,(H2,6,7,8)
SMILES string
OCC(COP(O)(O)=O)=O
InChI key
GNGACRATGGDKBX-UHFFFAOYSA-N
assay
≥95.0% (TLC)
form
powder
storage temp.
−20°C
Quality Level
Analysis Note
可能含有高达 2mol 当量的水
Biochem/physiol Actions
磷酸二羟丙酮（DHAP）是一种参与到多种通路中的代谢中间体，包括糖酵解、糖异生、甘油代谢、磷脂酸合成、脂肪代谢和卡尔文循环。
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
John P Richard
Biochemistry, 51(13), 2652-2661 (2012-03-14)
Triosephosphate isomerase (TIM) catalyzes the stereospecific 1,2-proton shift at dihydroxyacetone phosphate (DHAP) to give (R)-glyceraldehyde 3-phosphate through a pair of isomeric enzyme-bound cis-enediolate phosphate intermediates. The chemical transformations that occur at the active site of TIM were well understood by
Olga A Esakova et al.
Journal of the American Chemical Society, 141(36), 14142-14151 (2019-08-08)
Quinolinic acid is a common intermediate in the biosynthesis of nicotinamide adenine dinucleotide and its derivatives in all organisms that synthesize the molecule de novo. In most prokaryotes, it is formed from the condensation of dihydroxyacetone phosphate (DHAP) and iminoaspartate
Giovanni Covaleda-Cortés et al.
Marine drugs, 17(9) (2019-09-01)
A very powerful proteinaceous inhibitor of metallocarboxypeptidases has been isolated from the marine snail Nerita versicolor and characterized in depth. The most abundant of four, very similar isoforms, NvCla, was taken as reference and N-terminally sequenced to obtain a 372-nucleotide
Glycerolipid biosynthesis in peroxisomes via the acyl dihydroxyacetone phosphate pathway.
A K Hajra et al.
Annals of the New York Academy of Sciences, 386, 170-182 (1982-01-01)
Triosephosphate isomerase from human erythrocytes.
R W Gracy
Methods in enzymology, 41, 442-447 (1975-01-01)
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