产品名称
DL-threo-β-Methylaspartic acid,
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
assay
≥98% (TLC)
form
powder
color
white
Quality Level
Biochem/physiol Actions
DL-threo-β-Methylaspartic acid is an amino acid derivative.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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
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
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
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.
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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