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Merck
CN

M6126

DL-threo-β-Methylaspartic acid

≥98% (TLC)

别名:

2-Amino-3-methylsuccinic acid

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关于此项目

经验公式(希尔记法):
C5H9NO4
化学文摘社编号:
分子量:
147.13
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26
MDL number:
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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)


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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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
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

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