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Merck

A6262

Sigma-Aldrich

O-Acetyl-L-serine hydrochloride

Sinónimos:

O-acetyl-L-serine hydrochloride (1:1)

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About This Item

Fórmula empírica (notación de Hill):
C5H9NO4 · HCl
Número de CAS:
Peso molecular:
183.59
MDL number:
UNSPSC Code:
12352209
eCl@ss:
32160406
PubChem Substance ID:
NACRES:
NA.26

assay

≥98.0% (TLC)

Quality Level

form

powder

technique(s)

ligand binding assay: suitable

color

white to off-white

storage temp.

−20°C

SMILES string

Cl.CC(=O)OCC(N)C(O)=O

InChI

1S/C5H9NO4.ClH/c1-3(7)10-2-4(6)5(8)9;/h4H,2,6H2,1H3,(H,8,9);1H

InChI key

MGQOSZSPKMBSRW-UHFFFAOYSA-N

Biochem/physiol Actions

O-Acetyl-L-serine, a cysteine precursor, is used as a substrate for the identification, differentiation and characterization of O-acetyl-L-serine(thiol)lyase(s) (OASTL) involved in cysteine biosynthesis.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Anja Riemenschneider et al.
Plant physiology, 137(3), 892-900 (2005-02-25)
Plant cysteine (Cys) synthesis can occur in three cellular compartments: the chloroplast, cytoplasm, and mitochondrion. Cys formation is catalyzed by the enzyme O-acetylserine(thiol)lyase (OASTL) using O-acetylserine (OAS) and sulfide as substrates. To unravel the function of different isoforms of OASTL
Agnieszka Sirko et al.
Journal of experimental botany, 55(404), 1881-1888 (2004-06-23)
The last steps of cysteine biosynthesis are catalysed by a bi-enzyme complex composed of serine acetyltransferase (SAT) and cysteine synthase, also called O-acetyl-serine (thiol) lyase (OASTL). SAT is responsible for the production of O-acetyl-serine (OAS) from serine and acetyl-coenzyme A
CysK from Lactobacillus casei encodes a protein with O-acetylserine sulfhydrylase and cysteine desulfurization activity.
Bogicevic B, Berthoud H, et al.
Applied Microbiology and Biotechnology, 94(5), 1206-1220 (2011)
Haijun Zhao et al.
The New phytologist, 211(3), 926-939 (2016-04-26)
Two low phytic acid (lpa) mutants have been developed previously with the aim to improve the nutritional value of rice (Oryza sativa) grains. In the present study, the impacts of lpa mutations on grain composition and underlying molecular mechanisms were
Simona Carfagna et al.
Journal of plant physiology, 168(18), 2188-2195 (2011-09-17)
We analyzed the effects of deprivation and subsequent restoration of sulphate (S) in the nutrient solution on cysteine (Cys) and O-acetyl-L-serine (OAS) levels in Chlorella sorokiniana (211/8k). The removal of S from the culture medium caused a time-dependent increase in

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