A0876
N-Acetyl-D-leucine
≥99% (TLC), suitable for ligand binding assays and cell cutlure
别名:
N-acetyl-D-Leucine
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选择尺寸
关于此项目
经验公式（希尔记法）:
C8H15NO3
化学文摘社编号:
分子量:
173.21
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26
MDL number:
产品名称
N-Acetyl-D-leucine,
SMILES string
CC(C)C[C@@H](NC(C)=O)C(O)=O
InChI key
WXNXCEHXYPACJF-SSDOTTSWSA-N
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
assay
≥99% (TLC)
form
powder
technique(s)
cell culture | mammalian: suitable
ligand binding assay: suitable
color
white
storage temp.
−20°C
Quality Level
Application
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).
Biochem/physiol Actions
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.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
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
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
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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