M6001
α-Methyl-DL-aspartic acid
Sinónimos:
2-Amino-2-methylsuccinic acid
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About This Item
Fórmula empírica (notación de Hill):
C5H9NO4
Número de CAS:
Peso molecular:
147.13
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26
Productos recomendados
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
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
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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