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M6126

Sigma-Aldrich

DL-threo-β-Methylaspartic acid

≥98% (TLC)

Sinónimos:

2-Amino-3-methylsuccinic acid

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About This Item

Fórmula empírica (notación de Hill):
C5H9NO4
Número de CAS:
6667-60-3
Peso molecular:
147.13
MDL number:
MFCD00037770
UNSPSC Code:
12352209
PubChem Substance ID:
24897077
NACRES:
NA.26

product name

DL-threo-β-Methylaspartic acid,

assay

≥98% (TLC)

form

powder

color

white

SMILES string

CC(C(N)C(O)=O)C(O)=O

InChI

1S/C5H9NO4/c1-2(4(7)8)3(6)5(9)10/h2-3H,6H2,1H3,(H,7,8)(H,9,10)

InChI key

LXRUAYBIUSUULX-UHFFFAOYSA-N

Biochem/physiol Actions

DL-threo-β-Methylaspartic acid is an amino acid derivative.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Silke Schabbert et al.
Bioorganic & medicinal chemistry, 10(10), 3331-3337 (2002-08-02)
We report the synthesis and biological activity of a series of side-chain-constrained RGD peptides containing the (2S,3R) or (2S,3S) beta-methyl aspartic acid within the RGD sequence. These compounds have been assayed for binding to the integrin receptors alpha(IIb)beta3 and alpha(v)beta3
Jorge Heredia-Moya et al.
Bioorganic & medicinal chemistry, 16(11), 5908-5913 (2008-05-13)
Beta-(S-Methyl)thioaspartic acid occurs as a posttranslational modification at position 88 in Escherichia coli ribosomal protein S12, a position that is a mutational hotspot resulting in both antibiotic-resistant and antibiotic-sensitive phenotypes. Critical to research designed to determine the biological function of
Miryam Asuncion et al.
The Journal of biological chemistry, 277(10), 8306-8311 (2001-12-19)
Methylaspartate ammonia-lyase (3-methylaspartase, MAL; EC ) catalyzes the reversible anti elimination of ammonia from L-threo-(2S,3S)-3-methylaspartic acid to give mesaconic acid. This reaction lies on the main catabolic pathway for glutamate in Clostridium tetanomorphum. MAL requires monovalent and divalent cation cofactors
G F Short et al.
Biochemistry, 39(30), 8768-8781 (2000-07-29)
Aspartates 25 and 125, the active site residues of HIV-1 protease, participate functionally in proteolysis by what is believed to be a general acid-general base mechanism. However, the structural role that these residues may play in the formation and maintenance
N P Botting et al.
Biochemistry, 31(5), 1509-1520 (1992-02-11)
The enzyme 3-methylaspartate ammonia-lyase (EC 4.3.1.2) catalyzes the exchange of the C-3 hydrogen of the substrate, (2S,3S)-3-methylaspartic acid, with solvent hydrogen. The mechanism of the exchange reaction was probed using (2S,3S)-3-methylaspartic acid and its C-3-deuteriated isotopomer. Incubations conducted in tritiated
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Chromatograms

application for HPLC

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