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Merck

04668

Sigma-Aldrich

O-Phospho-L-homoserin Lithiumsalz

≥95% (TLC)

Synonym(e):

O-Phosphono-L-homoserin Lithiumsalz, L-2-Amino-4-hydroxybuttersäure-4-phosphat Lithiumsalz, L-Homoserin-O-phosphat Lithiumsalz, H-Hse(PO3H2)-OH

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About This Item

Empirische Formel (Hill-System):
C4H10NO6P · xLi+
CAS-Nummer:
Molekulargewicht:
199.10 (free acid basis)
UNSPSC-Code:
12352209
NACRES:
NA.26

Assay

≥95% (TLC)

Form

powder

Optische Aktivität

[α]/D -18.0±2.0°, c = 1 in H2O

Farbe

white to off-white

Lagertemp.

−20°C

InChI

1S/C4H10NO6P/c5-3(4(6)7)1-2-11-12(8,9)10/h3H,1-2,5H2,(H,6,7)(H2,8,9,10)/t3-/m0/s1

InChIKey

FXDNYOANAXWZHG-VKHMYHEASA-N

Biochem./physiol. Wirkung

Metabolite in glycine, serine and threonine metabolism. In higher plants, O-phosphohomoserine represents a branch point between the methionine and threonine biosynthetic pathways.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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Stereochemistry of the hydrogen removal at position 3 in the enzymic synthesis of L-threonine from O-phospho-L-homoserine.
Fuganti, C.
Journal of the Chemical Society. Chemical Communications, 7, 337-339 (1979)
An ATP-independent phosphotransferase in higher plants. The formation of O-phospho-L-homoserine from O-succinyl-L-homoserine and phosphate.
Haginiwa, J., et al.
Chemical & Pharmaceutical Bulletin, 27, 1710-1713 (1979)
Oliver Kreft et al.
Plant physiology, 131(4), 1843-1854 (2003-04-15)
In plants, metabolic pathways leading to methionine (Met) and threonine diverge at the level of their common substrate, O-phosphohomoserine (OPHS). To investigate the regulation of this branch point, we engineered transgenic potato (Solanum tuberosum) plants affected in cystathionine gamma-synthase (CgS)
D Bartlem et al.
Plant physiology, 123(1), 101-110 (2000-05-12)
In higher plants, O-phosphohomoserine (OPH) represents a branch point between the methionine (Met) and threonine (Thr) biosynthetic pathways. It is believed that the enzymes Thr synthase (TS) and cystathionine gamma-synthase (CGS) actively compete for the OPH substrate for Thr and
G E Gilbert et al.
Biochemistry, 32(37), 9577-9585 (1993-09-21)
Phosphatidylserine, a negatively charged lipid, is exposed on the platelet membrane following cell stimulation, correlating with the expression of factor VIII receptors. We have explored the importance of the negative electrostatic potential of phosphatidylserine vs chemical moieties of phosphatidylserine for

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