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Merck

E0377

Sigma-Aldrich

D-Erythrose 4-phosphate sodium salt

≥50% (TLC)

Szinonimák:

4-Phospho-D-erythrose sodium salt

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

Tapasztalati képlet (Hill-képlet):
C4H8NaO7P
CAS-szám:
Molekulatömeg:
222.07
UNSPSC kód:
12352201
NACRES:
NA.25

Minőségi szint

Teszt

≥50% (TLC)

form

powder

szín

white to off-white

oldhatóság

water: 50 mg/mL, clear to slightly hazy, colorless to faintly yellow

tárolási hőmérséklet

−20°C

SMILES string

[Na+].[H]C(=O)[C@H](O)[C@H](O)COP(O)([O-])=O

InChI

1S/C4H9O7P.Na/c5-1-3(6)4(7)2-11-12(8,9)10;/h1,3-4,6-7H,2H2,(H2,8,9,10);/q;+1/p-1/t3-,4+;/m0./s1

Nemzetközi kémiai azonosító kulcs

KKDBADMPNGAKHM-RFKZQXLXSA-M

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Alkalmazás

D-Erythrose 4-phosphate (E4P) is used as a substrate to identify, differentiate and characterize 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolase(s) and 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) synthase(s) that initiate the shikimate pathway in microorganisms and plants. It may be used as a substrate to identify, differentiate and characterize glyceraldehyde-3-phosphate dehydrogenase(s) (GAPDH) involved in surface antigen and virulence factor development in pathogenic microorganisms. E4P may be used in malaria research as an inhibitor of the PfPdx1 component of the PLP (pyridoxal 5′-phosphate) synthase enzymatic complex responsible for the de novo synthesizes vitamin B6 in Plasmodium falciparum.

Biokémiai/fiziológiai hatások

Erythrose 4-phosphate is an intermediate in the penntose phosphate pathway, as well as the biosynthesis of phenylalanine, tyrosine, tryptophan and metabolism of vitamin B6.

Egyéb megjegyzések

To gain a comprehensive understanding of our extensive range of Monosaccharides for your research, we encourage you to visit our Carbohydrates Category page.

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

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Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

J Bongaerts et al.
Metabolic engineering, 3(4), 289-300 (2001-10-26)
Metabolic engineering to design and construct microorganisms suitable for the production of aromatic amino acids and derivatives thereof requires control of a complicated network of metabolic reactions that partly act in parallel and frequently are in rapid equilibrium. Engineering the
Ingrid B Müller et al.
PloS one, 4(2), e4406-e4406 (2009-02-07)
The human malaria parasite Plasmodium falciparum is able to synthesize de novo pyridoxal 5-phosphate (PLP), a crucial cofactor, during erythrocytic schizogony. However, the parasite possesses additionally a pyridoxine/pyridoxal kinase (PdxK) to activate B6 vitamers salvaged from the host. We describe
David Tran et al.
Bioorganic & medicinal chemistry letters, 21(22), 6838-6841 (2011-10-08)
3-Deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) synthase catalyses the first step of the shikimate pathway, which is responsible for the biosynthesis of aromatic amino acids in microorganisms and plants. This enzyme catalyses an aldol reaction between phosphoenolpyruvate and D-erythrose 4-phosphate to generate DAH7P.
Bouchra Elkhalfi et al.
Protein expression and purification, 89(2), 146-155 (2013-03-20)
The gammaproteobacterium Pseudomonas syringae pv. tomato DC3000 is the causal agent of bacterial speck, a common disease of tomato. The mode of infection of this pathogen is not well understood, but according to molecular biological, genomic and proteomic data it
Shaun B Reeksting et al.
The Biochemical journal, 449(1), 175-187 (2012-10-09)
Malaria tropica is a devastating infectious disease caused by Plasmodium falciparum. This parasite synthesizes vitamin B6 de novo via the PLP (pyridoxal 5'-phosphate) synthase enzymatic complex consisting of PfPdx1 and PfPdx2 proteins. Biosynthesis of PLP is largely performed by PfPdx1

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