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Key Documents

M6001

Sigma-Aldrich

α-甲基-DL-天冬氨酸

同義詞:

2-氨基-2-甲基琥珀酸

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About This Item

經驗公式(希爾表示法):
C5H9NO4
CAS號碼:
分子量::
147.13
MDL號碼:
分類程式碼代碼:
12352209
PubChem物質ID:
NACRES:
NA.26

化驗

≥98% (TLC)

形狀

powder

顏色

white

SMILES 字串

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 密鑰

CWAYDJFPMMUKOI-UHFFFAOYSA-N

生化/生理作用

α-甲基-dl-天冬氨酸是内皮细胞NO和I-瓜氨酸生成的I抑制剂。

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


分析證明 (COA)

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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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