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About This Item
Linear Formula:
C6H5CH2SCH2CH(NH2)CO2H
CAS Number:
Molecular Weight:
211.28
NACRES:
NA.22
PubChem Substance ID:
eCl@ss:
32160406
UNSPSC Code:
12352209
EC Number:
221-273-4
MDL number:
Beilstein/REAXYS Number:
1879358
InChI key
GHBAYRBVXCRIHT-VIFPVBQESA-N
InChI
1S/C10H13NO2S/c11-9(10(12)13)7-14-6-8-4-2-1-3-5-8/h1-5,9H,6-7,11H2,(H,12,13)/t9-/m0/s1
SMILES string
N[C@@H](CSCc1ccccc1)C(O)=O
assay
97%
form
powder
optical activity
[α]20/D +23°, c = 2 in 1 M NaOH
reaction suitability
reaction type: solution phase peptide synthesis
color
white to off-white
mp
214 °C (dec.) (lit.)
application(s)
detection
peptide synthesis
Quality Level
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Storage Class
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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Michelle Rudden et al.
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M Rooseboom et al.
Chemical research in toxicology, 14(1), 127-134 (2001-02-15)
Previously, it was shown that beta-elimination of selenocysteine Se-conjugates by rat renal cytosol leading to pyruvate formation was not solely catalyzed by pyridoxal phosphate-dependent enzymes. It was hypothesized that selenoxidation of the selenocysteine Se-conjugates, followed by syn-elimination, may be an
A Heuner et al.
Pflugers Archiv : European journal of physiology, 417(5), 523-527 (1991-01-01)
We investigated the capacity and the localization of N-acetylation of the mercapturic acid precursor S-benzyl-L-cysteine (BC), as well as the tubular reabsorption of this compound in the rat kidney in vivo et situ by renal clearance and continuous microinfusion and
R S Phillips et al.
The Journal of biological chemistry, 266(28), 18642-18648 (1991-10-05)
Lysine 269 in Escherichia coli tryptophan indole-lyase (tryptophanase) has been changed to arginine by site-directed mutagenesis. The resultant K269R mutant enzyme exhibits kcat values about 10% those of the wild-type enzyme with S-(o-nitrophenyl)-L-cysteine, L-tryptophan, and S-benzyl-L-cysteine, while kcat/Km values are
P J Sausen et al.
The Journal of biological chemistry, 265(11), 6139-6145 (1990-04-15)
Cysteine conjugate S-oxidase activity, with S-benzyl-L-cysteine as substrate, was found mostly in the microsomal fractions of rat liver and kidney. In the presence of oxygen and NADPH, S-benzyl-L-cysteine is converted to S-benzyl-L-cysteine sulfoxide; no S-benzyl-L-cysteine sulfone was detected. The Vmax
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