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Key Documents

M6001

Sigma-Aldrich

α-Methyl-DL-aspartic acid

Synonym(s):

2-Amino-2-methylsuccinic acid

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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
Pricing and availability is not currently available.

Assay

≥98% (TLC)

form

powder

color

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)

InChI key

CWAYDJFPMMUKOI-UHFFFAOYSA-N

Biochem/physiol Actions

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

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

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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
Victor Sourjik et al.
Proceedings of the National Academy of Sciences of the United States of America, 99(1), 123-127 (2001-12-14)
Chemoreceptors in Escherichia coli are coupled to the flagella by a labile phosphorylated intermediate, CheY approximately P. Its activity can be inferred from the rotational bias of flagellar motors, but motor response is stochastic and limited to a narrow physiological
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
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.

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