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Merck

A0876

Sigma-Aldrich

N-Acetyl-D-leucine

≥99% (TLC), suitable for ligand binding assays and cell cutlure

别名:

N-acetyl-D-Leucine

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About This Item

经验公式(希尔记法):
C8H15NO3
CAS号:
分子量:
173.21
MDL號碼:
分類程式碼代碼:
12352209
PubChem物質ID:
NACRES:
NA.26

product name

N-Acetyl-D-leucine,

化驗

≥99% (TLC)

形狀

powder

技術

cell culture | mammalian: suitable
ligand binding assay: suitable

顏色

white

儲存溫度

−20°C

SMILES 字串

CC(C)C[C@@H](NC(C)=O)C(O)=O

InChI

1S/C8H15NO3/c1-5(2)4-7(8(11)12)9-6(3)10/h5,7H,4H2,1-3H3,(H,9,10)(H,11,12)/t7-/m1/s1

InChI 密鑰

WXNXCEHXYPACJF-SSDOTTSWSA-N

應用

N-Acetyl-D-leucine may be used with other D-aminoacylated amino acids as a substrate for the identification, differentiation and characterization of D-aminoacylase(s)/amidohydrolase(s).

生化/生理作用

N-Acetyl-D-leucine is a substrate for D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. N-Acetyl-D-leucine is used to help differentiate members of the amidohydrolase enzyme superfamily. It is a preferred substrate of Gox1177 from Gluconobacter oxidans.

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)


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Y B Yang et al.
Bioscience, biotechnology, and biochemistry, 56(9), 1392-1395 (1992-09-01)
The D-aminoacylase produced by Alcaligenes denitrificans DA181 was a new type of aminoacylase which had both high stereospecificity and specific activity. The molecular weight and isoelectric point of this enzyme were 58,000 and 4.4, respectively. The apparent Km and kcat
M Moriguchi et al.
Bioscience, biotechnology, and biochemistry, 57(7), 1149-1152 (1993-07-01)
The best inducers for D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 (Alcaligenes A-6) were a poor substrate, N-acetyl-gamma-methyl-D-leucine, and an inhibitor, N-acetyl-D-alloisoleucine. The enzyme has been homogeneously purified. The molecular weight of the native enzyme was estimated to be 58,000
Jennifer A Cummings et al.
Biochemistry, 48(27), 6469-6481 (2009-06-13)
The catalytic activities of three members of the amidohydrolase superfamily were discovered using amino acid substrate libraries. Bb3285 from Bordetella bronchiseptica, Gox1177 from Gluconobacter oxidans, and Sco4986 from Streptomyces coelicolor are currently annotated as d-aminoacylases or N-acetyl-d-glutamate deacetylases. These three

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