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Merck

A2636

S-(2-Aminoethyl)-L-cysteine hydrochloride

≥98% (TLC)

Synonyme(s) :

L-4-Thialysine hydrochloride

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About This Item

Formule empirique (notation de Hill) :
C5H12N2O2S · HCl
Numéro CAS:
Poids moléculaire :
200.69
NACRES:
NA.26
PubChem Substance ID:
eCl@ss:
32160406
UNSPSC Code:
12352209
EC Number:
223-862-1
MDL number:
Beilstein/REAXYS Number:
3697262

Nom du produit

S-(2-Aminoethyl)-L-cysteine hydrochloride, ≥98% (TLC)

InChI

1S/C5H12N2O2S.ClH/c6-1-2-10-3-4(7)5(8)9;/h4H,1-3,6-7H2,(H,8,9);1H/t4-;/m0./s1

InChI key

CVHKULVNPGAEQM-WCCKRBBISA-N

SMILES string

Cl.NCCSC[C@H](N)C(O)=O

assay

≥98% (TLC)

form

powder

color

white to off-white

storage temp.

2-8°C

Quality Level

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Biochem/physiol Actions

S-(2-Aminoethyl)-L-cysteine (AEC) hydrochloride is used as a lysine analogue for comparative analysis with other lysine analogues. S-(2-Aminoethyl)-L-cysteine is an alternative substrate useful for characterizing lysine cyclodeaminase from Streptomyces pristinaespiralis. AEC may be used as a non-antibiotic selection agent for genetically engineered soybeans expressing a lysine insensitive DHPS gene. AEC is being studied as an amino acid antibiotic.

Classe de stockage

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Yuko Kanemaru et al.
Journal of bacteriology, 195(17), 3845-3853 (2013-06-25)
Thermus thermophilus exhibits hypersensitivity to a lysine analog, (S)-2-aminoethyl-cysteine (AEC). Cosmid libraries were constructed using genomes from two AEC-resistant mutants, AT10 and AT14, and the cosmids that conferred AEC resistance on the wild-type strain were isolated. When the cosmid library
Ayako Yoshida et al.
Journal of molecular biology, 368(2), 521-536 (2007-03-14)
Aspartate kinase (AK) catalyzes the first step of the biosynthesis of the aspartic acid family amino acids, and is regulated via feedback inhibition by end-products including Thr and Lys. To elucidate the mechanism of this inhibition, we determined the crystal
Sandro F Ataide et al.
ACS chemical biology, 2(12), 819-827 (2007-12-25)
Structural and functional diversity among the aminoacyl-tRNA synthetases prevent infiltration of the genetic code by noncognate amino acids. To explore whether these same features distinguish the synthetases as potential sources of resistance against antibiotic amino acid analogues, we investigated bacterial
Anne Daly et al.
Nutrients, 12(8) (2020-08-23)
In Phenylketonuria (PKU), the peptide structure of the protein substitute (PS), casein glycomacropeptide (CGMP), is supplemented with amino acids (CGMP-AA). CGMP may slow the rate of amino acid (AA) absorption compared with traditional phenylalanine-free amino acids (Phe-free AA), which may
Asri Peni Wulandari et al.
FEBS letters, 522(1-3), 35-40 (2002-07-04)
In Thermus thermophilus homocitrate synthase (HCS) catalyzes the initial reaction of lysine biosynthesis through alpha-aminoadipic acid, synthesis of homocitrate from 2-oxoglutarate and acetyl-CoA. HCS is strongly inhibited by lysine, indicating that the biosynthesis is regulated by the endproduct at the

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