T1660
Nε,Nε,Nε-Trimethyllysine hydrochloride
≥97% (TLC)
Synonym(s):
1-Pentanaminium, 5-amino-5-carboxy-N,N,N-trimethyl-, chloride (1:1), (5S)-
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About This Item
Empirical Formula (Hill Notation):
C9H20N2O2 · HCl
CAS Number:
Molecular Weight:
224.73
MDL number:
UNSPSC Code:
12352202
PubChem Substance ID:
NACRES:
NA.26
Recommended Products
Assay
≥97% (TLC)
form
powder
contains
salts and water as balance
composition
Amino acid content, ~75%
technique(s)
LC/MS: suitable
color
white
storage temp.
−20°C
SMILES string
[Cl-].C[N+](C)(C)CCCC[C@H](N)C(O)=O
InChI
1S/C9H20N2O2.ClH/c1-11(2,3)7-5-4-6-8(10)9(12)13;/h8H,4-7,10H2,1-3H3;1H/t8-;/m0./s1
InChI key
ZKIJKCHCMFGMCM-QRPNPIFTSA-N
Related Categories
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Molecular carcinogenesis, 47(9), 701-706 (2008-01-08)
Methylation of lysine 27 on histone H3 (H3K27) by the EZH2 complex is an epigenetic mark that mediates gene silencing. EZH2 is overexpressed in many cancers and correlates with poor prognosis in both breast and prostate cancers. However, the status
Naomi van Vlies et al.
The FEBS journal, 274(22), 5845-5851 (2007-10-20)
The first enzyme of carnitine biosynthesis is the mitochondrial 6-N-trimethyllysine dioxygenase, which converts 6-N-trimethyllysine to 3-hydroxy-6-N-trimethyllysine. Using progressive membrane solubilization with digitonin and protease protection experiments, we show that this enzyme is localized in the mitochondrial matrix. Latency experiments with
Maren Fischer et al.
The British journal of nutrition, 101(2), 190-196 (2008-05-22)
This study was performed to investigate whether dietary lysine concentration influences the carnitine status of pigs. Therefore, an experiment with twenty young pigs with an average body weight of 21 kg was performed which were fed either a control diet
Lynnette M A Dirk et al.
Biochemistry, 46(12), 3905-3915 (2007-03-07)
Processive versus distributive methyl group transfer was assessed for pea Rubisco large subunit methyltransferase, a SET domain protein lysine methyltransferase catalyzing the formation of trimethyllysine-14 in the large subunit of Rubisco. Catalytically competent complexes between an immobilized form of des(methyl)
Jean-François Couture et al.
The Journal of biological chemistry, 281(28), 19280-19287 (2006-05-10)
SET domain enzymes represent a distinct family of protein lysine methyltransferases in eukaryotes. Recent studies have yielded significant insights into the structural basis of substrate recognition and the product specificities of these enzymes. However, the mechanism by which SET domain
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