69312
L-Glyceraldehyde-3-phosphate solution
≥95% (TLC), 8-12 mg/mL in H2O (qNMR)
别名:
(2S)-2-Hydroxy-3-phosphonooxypropanal, L-GAP
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选择尺寸
关于此项目
经验公式（希尔记法）:
C3H7O6P
化学文摘社编号:
分子量:
170.06
NACRES:
NA.25
PubChem Substance ID:
UNSPSC Code:
12352201
MDL number:
产品名称
L-Glyceraldehyde-3-phosphate solution, ≥95% (TLC), 8-12 mg/mL in H2O (qNMR)
InChI
1S/C3H7O6P/c4-1-3(5)2-9-10(6,7)8/h1,3,5H,2H2,(H2,6,7,8)/t3-/m1/s1
SMILES string
[H]C([C@@H](O)COP(O)(O)=O)=O
InChI key
LXJXRIRHZLFYRP-GSVOUGTGSA-N
assay
≥95% (TLC)
form
liquid
concentration
8-12 mg/mL in H2O (qNMR)
impurities
≤0.5 mg/mL D-glyceraldehyde-3-phosphate (enzymatic)
storage temp.
−20°C
Quality Level
Biochem/physiol Actions
L-Glyceraldehyde 3-phosphate is a potent non-competitive inhibitor of NADP-dependent non-phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase and a substrate for L-Glyceraldehyde 3-phosphate reductase.
Other Notes
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存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
C T Tang et al.
Antimicrobial agents and chemotherapy, 11(1), 147-153 (1977-01-01)
At a concentration of 2.5 mM, dl-glyceraldehyde 3-phosphate has a bactericidal effect upon Escherichia coli. The glycerol 3-phosphate transport system is required for the entry of the biologically active l-enantiomer. l-Glyceraldehyde must be phosphorylated by the cell to exert its
A Hall et al.
Biochemistry, 14(19), 4348-4353 (1975-09-23)
By a combination of methods involving enzyme-catalyzed reactions and classical iodination techniques it has been possible to obtain all the relevant rate constants for the uncatalyzed interconversion of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate via their common enediol intermediate. These rate
J P Richard
Biochemistry, 24(4), 949-953 (1985-02-12)
Triosephosphate isomerase catalyzes the isomerization and/or racemization reactions of L-glyceraldehyde 3-phosphate (LGAP), the enantiomer of the physiological substrate. The reaction is inhibited by the active site directed reagent glycidol phosphate. The amount of protonation product formation catalyzed by a fixed
Purification and properties of NADP-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the green alga Chlamydomonas reinhardtii.
Iglesias, A.A., et al.
Biochimica et Biophysica Acta, 925, 1-10 (1987)
Kevin K Desai et al.
Bioorganic chemistry, 38(1), 37-41 (2009-12-18)
Recently, we reported that YghZ from Escherichia coli functions as an efficient L-glyceraldehyde 3-phosphate reductase (Gpr). Here we show that Gpr co-purifies with a b-type heme cofactor. Gpr associates with heme in a 1:1 stoichiometry to form a complex that
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