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Key Documents

M6126

Sigma-Aldrich

DL-threo-β-Methylaspartic acid

≥98% (TLC)

Synonyme(s) :

2-Amino-3-methylsuccinic acid

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About This Item

Formule empirique (notation de Hill):
C5H9NO4
Numéro CAS:
Poids moléculaire :
147.13
Numéro MDL:
Code UNSPSC :
12352209
ID de substance PubChem :
Nomenclature NACRES :
NA.26

product name

DL-threo-β-Methylaspartic acid,

Pureté

≥98% (TLC)

Niveau de qualité

Forme

powder

Couleur

white

Chaîne SMILES 

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)

Clé InChI

LXRUAYBIUSUULX-UHFFFAOYSA-N

Actions biochimiques/physiologiques

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

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

P Madhavapeddi et al.
Chemistry & biology, 8(12), 1143-1149 (2002-01-05)
Adenosylcobalamin (coenzyme B(12))-dependent enzymes catalyze a variety of chemically difficult reactions that proceed through the generation of free radical intermediates. A long-standing question is how proteins stabilize what are normally regarded as highly reactive organic radicals and direct them towards
Y Asano et al.
FEMS microbiology letters, 118(3), 255-258 (1994-05-15)
Crystalline 3-methylaspartase (EC 4.3.1.2) from Escherichia coli strain YG1002 that had been isolated from soil was characterized. The enzyme activity was induced when the organism was grown statically on medium containing (S)-glutamic acid. Its molecular mass is about 84 kDa
Amanda J Brooks et al.
Biochemistry, 44(46), 15167-15181 (2005-11-16)
Glutamate mutase (GM) is a cobalamin-dependent enzyme that catalyzes the reversible interconversion of L-glutamate and L-threo-3-methylaspartate via a radical-based mechanism. To initiate catalysis, the 5'-deoxyadenosylcobalamin (AdoCbl) cofactor's Co-C bond is cleaved homolytically to generate an adenosyl radical and Co2+ Cbl.
S L Bearne et al.
Molecular and cellular biochemistry, 221(1-2), 117-126 (2001-08-17)
Beta-methylaspartase (EC 4.3.1.2) was purified 20-fold in 35% yield from Fusobacterium varium, an obligate anaerobe. The purification steps included heat treatment, fractional precipitation with ammonium sulfate and ethanol, gel filtration, and ion exchange chromatography on DEAE-Sepharose. The enzyme is dimeric
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

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