DL-glyceraldehyde 3-phosphate
DL-glyceraldehyde 3-phosphate structure
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Common Name | DL-glyceraldehyde 3-phosphate | ||
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| CAS Number | 20283-52-7 | Molecular Weight | 170.05800 | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | C3H7O6P | Melting Point | N/A | |
| MSDS | N/A | Flash Point | N/A | |
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The uncatalyzed rates of enolization of dihydroxyacetone phoshate and of glyceraldehyde 3-phosphate in neutral aqueous solution. The quantitative assessment of the effectiveness of an enzyme catalyst.
Biochemistry 14(19) , 4348-53, (1975) 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-phosph... |
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L-Glyceraldehude 3-phosphate, a bactericidal agent.
Antimicrob. Agents Chemother. 11(1) , 147-53, (1977) 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 b... |
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Reaction of triosephosphate isomerase with L-glyceraldehyde 3-phosphate and triose 1,2-enediol 3-phosphate.
Biochemistry 24(4) , 949-53, (1985) 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 am... |
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L-glyceraldehyde 3-phosphate reductase from Escherichia coli is a heme binding protein.
Bioorg. Chem. 38(1) , 37-41, (2010) 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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Purification and properties of NADP-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the green alga Chlamydomonas reinhardtii. Iglesias, A.A., et al.
Biochim. Biophys. Acta 925 , 1-10, (1987)
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