M6126
DL-threo-β-Methylaspartic acid
≥98% (TLC)
Synonym(s):
2-Amino-3-methylsuccinic acid
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All Photos(2)
About This Item
Empirical Formula (Hill Notation):
C5H9NO4
CAS Number:
Molecular Weight:
147.13
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26
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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 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
Certificates of Analysis (COA)
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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
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
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
Chromatograms
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