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3,3,3-Trifluor-DL-alanin
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100 MG
CHF 51.80
About This Item
Lineare Formel:
CF3CH(NH2)CO2H
CAS-Nummer:
Molekulargewicht:
143.06
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352209
PubChem Substanz-ID:
NACRES:
NA.22
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Qualitätsniveau
Assay
98%
Eignung der Reaktion
reaction type: solution phase peptide synthesis
mp (Schmelzpunkt)
231-234 °C (lit.)
Anwendung(en)
peptide synthesis
Lagertemp.
2-8°C
SMILES String
NC(C(O)=O)C(F)(F)F
InChI
1S/C3H4F3NO2/c4-3(5,6)1(7)2(8)9/h1H,7H2,(H,8,9)
InChIKey
HMJQKIDUCWWIBW-UHFFFAOYSA-N
Verwandte Kategorien
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Persönliche Schutzausrüstung
dust mask type N95 (US), Eyeshields, Gloves
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R S Phillips et al.
Archives of biochemistry and biophysics, 296(2), 489-496 (1992-08-01)
Trifluoroalanine is a mechanism-based inactivator of Escherichia coli tryptophan indole-lyase (tryptophanase) and E. coli tryptophan synthase (R. B. Silverman and R. H. Abeles, 1976, Biochemistry 15, 4718-4723). We have found that indole is able to prevent inactivation of tryptophan indole-lyase
C W Fearon et al.
Biochemistry, 21(16), 3790-3794 (1982-08-03)
Inactivation of gamma-cystathionase by beta, beta, beta-trifluoroalanine, a suicide inactivator of the enzyme, results in covalent labeling of an amino group of the protein [Silverman, R. B., & Abeles, R. H. (1977) Biochemistry 16, 5515-5520]. We have established that this
W S Faraci et al.
Biochemistry, 28(2), 431-437 (1989-01-24)
The alanine racemases are a group of PLP-dependent bacterial enzymes that catalyze the racemization of alanine, providing D-alanine for cell wall synthesis. Inactivation of the alanine racemases from the Gram-negative organism Salmonella typhimurium and Gram-positive organism Bacillus stearothermophilus with beta
E A Wang et al.
Biochemistry, 20(26), 7539-7546 (1981-12-22)
The alanine racemase from Escherichia coli B has been shown to process DL isomers of beta -fluoroalanine as suicide substrates with an identical partitioning ratio for each enantiomer of 820 catalytic eliminations of HF per enzymatic inactivation event [Wang, E.
T Clausen et al.
Journal of molecular biology, 262(2), 202-224 (1996-09-20)
Cystathionine beta-lyase (CBL) is a member of the gamma-family of PLP-dependent enzymes, that cleaves C beta-S bonds of a broad variety of substrates. The crystal structure of CBL from E. coli has been solved using MIR phases in combination with
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