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M6001

Sigma-Aldrich

α-Methyl-DL-aspartic acid

Synonym(e):

2-Amino-2-methylsuccinic acid

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About This Item

Empirische Formel (Hill-System):
C5H9NO4
CAS-Nummer:
2792-66-7
Molekulargewicht:
147.13
MDL-Nummer:
MFCD00056709
UNSPSC-Code:
12352209
PubChem Substanz-ID:
24897063
NACRES:
NA.26

Assay

≥98% (TLC)

Form

powder

Farbe

white

SMILES String

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

InChI

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

InChIKey

CWAYDJFPMMUKOI-UHFFFAOYSA-N

Biochem./physiol. Wirkung

α-methyl-dl-aspartic acid is an iinhibitor of endothelial NO and l-citrulline production.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)

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Xuejun Zhu et al.
Physical review letters, 108(12), 128101-128101 (2012-05-01)
We study Escherichia coli chemotaxis behavior in environments with spatially and temporally varying attractant sources by developing a unique microfluidic system. Our measurements reveal a frequency-dependent chemotaxis behavior. At low frequency, the E. coli population oscillates in synchrony with the attractant.
Harm Maarsingh et al.
European journal of pharmacology, 546(1-3), 171-176 (2006-08-22)
Nitric oxide synthase (NOS) converts L-arginine into nitric oxide (NO) and L-citrulline. In NO-producing cells, L-citrulline can be recycled to L-arginine in a two-step reaction involving argininosuccinate synthase (ASS) and -lyase (ASL). In guinea pig trachea, L-arginine is a limiting
Intrinsic deuterium kinetic isotope effects in glutamate mutase measured by an intramolecular competition experiment.
Miri Yoon et al.
Angewandte Chemie (International ed. in English), 46(44), 8455-8459 (2007-10-03)
S Rhee et al.
The Journal of biological chemistry, 272(28), 17293-17302 (1997-07-11)
Two high resolution crystal structures of cytosolic aspartate aminotransferase from pig heart provide additional insights into the stereochemical mechanism for ligand-induced conformational changes in this enzyme. Structures of the homodimeric native structure and its complex with the substrate analog 2-methylaspartate
J Jäger et al.
Journal of molecular biology, 239(2), 285-305 (1994-06-03)
Three crystal structures of wild type E. coli aspartate aminotransferase (E.C.2.6.1.1) in space group P2(1) have been determined at resolution limits between 2.6 and 2.35 A. The unliganded enzyme and its complexes with the substrate analogues maleate and 2-methylaspartate resulted
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