A6262
O-Acetyl-L-serine hydrochloride
Synonym(s):
O-acetyl-L-serine hydrochloride (1:1)
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About This Item
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Assay
≥98.0% (TLC)
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 Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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CysK from Lactobacillus casei encodes a protein with O-acetylserine sulfhydrylase and cysteine desulfurization activity.
Applied Microbiology and Biotechnology, 94(5), 1206-1220 (2011)
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
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
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
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
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