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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
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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Body odour is a characteristic trait of Homo sapiens, however its role in human behaviour and evolution is poorly understood. Remarkably, body odour is linked to the presence of a few species of commensal microbes. Herein we discover a bacterial
[Synthesis and antifibrinolytic activity of dipeptides of E-aminocaproic acid and sulfur-containing amino acids].
K Midura-Nowaczek et al.
Acta poloniae pharmaceutica, 45(1), 35-41 (1988-01-01)
A A Elfarra
Chemico-biological interactions, 96(1), 47-55 (1995-04-28)
Several xenobiotics and their corresponding cysteine S-conjugates are metabolized in vivo to cysteine S-conjugate sulfoxides and/or N-acetylcysteine S-conjugate sulfoxides. Homocysteine S-conjugates, such as methionine and ethionine, are also metabolized in vivo to sulfoxides. The enzymatic basis for these metabolic reactions
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
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
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