61837
DL-tert-Leucine
puriss., ≥99.0% (NT)
Synonym(s):
(±)-2-Amino-3,3-dimethylbutyric acid, DL-α-tert-Butylglycine
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About This Item
Linear Formula:
(CH3)3CCH(NH2)COOH
CAS Number:
Molecular Weight:
131.17
PubChem Substance ID:
UNSPSC Code:
12352200
Beilstein/REAXYS Number:
1721823
MDL number:
grade
puriss.
assay
≥99.0% (NT)
ign. residue
≤0.05%
mp
>300 °C (lit.)
solubility
H2O: 0.1 g/mL, clear, colorless
SMILES string
CC(C)(C)C(N)C(O)=O
InChI
1S/C6H13NO2/c1-6(2,3)4(7)5(8)9/h4H,7H2,1-3H3,(H,8,9)
InChI key
NPDBDJFLKKQMCM-UHFFFAOYSA-N
Storage Class
13 - Non 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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Fernando Formaggio et al.
Chemistry (Weinheim an der Bergstrasse, Germany), 11(8), 2395-2404 (2005-01-26)
Terminally protected homopeptides of tert-leucine, from the dimer to the hexamer, co-oligopeptides of tert-leucine in combination with alpha-aminoisobutyric acid or glycine residues up to the hexamer level, and simple dipeptides representing known scaffolds for catalysts in asymmetric organic reactions were
Philippe Bisel et al.
Organic & biomolecular chemistry, 6(15), 2655-2665 (2008-07-18)
The unique reactivity pattern elicited by the crowded tert-butyl group is highlighted by summarising characteristic applications. Starting from the use of this simple hydrocarbon moiety in chemical transformations, via its relevance in Nature and its implication in biosynthetic and biodegradation
Stabilizing and destabilizing effects of placing beta-branched amino acids in protein alpha-helices.
V W Cornish et al.
Biochemistry, 33(40), 12022-12031 (1994-10-11)
In order to gain greater insight into the effects of beta-branched amino acids on protein alpha-helices, hydrophobic amino acids with varying degrees of beta-branching, including the fully beta-substituted L-2-amino-3,3-dimethylbutanoic acid (ADBA), were incorporated into the protein T4 lysozyme. The unnatural
Shu-Lai Liu et al.
Bioprocess and biosystems engineering, 28(5), 285-289 (2005-10-26)
Penicillin G acylase (PGA) from Kluyvera citrophila immobilized on Amberzyml was used for enantioselective hydrolysis of N-phenylacetylated-DL-tert-leucine (N-Phac-DL-Tle) to produce L-tert-leucine (L-Tle). The effects of various organic cosolvents on hydrolysis of N-Phac-DL-Tle have been investigated in aqueous-cosolvent medium. It was
K Laumen et al.
Bioscience, biotechnology, and biochemistry, 65(9), 1977-1980 (2001-10-26)
Optically pure D-tert.-leucine was obtained by the enzymatic hydrolysis of (+/-)-N-acetyl-tert. leucine chloroethyl ester after about 50% conversion, this being catalyzed by a protease from Bacillus licheniformis (Alcalase), and subsequent acidic saponification of the recovered ester. Among the methyl, ethyl
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