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A0876

Sigma-Aldrich

N-Acetyl-D-leucine

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

Synonym(s):

N-acetyl-D-Leucine

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About This Item

Empirical Formula (Hill Notation):
C8H15NO3
CAS Number:
19764-30-8
Molecular Weight:
173.21
MDL number:
MFCD00066069
UNSPSC Code:
12352209
PubChem Substance ID:
24890460
NACRES:
NA.26

product name

N-Acetyl-D-leucine,

assay

≥99% (TLC)

form

powder

technique(s)

cell culture | mammalian: suitable
ligand binding assay: suitable

color

white

storage temp.

−20°C

SMILES string

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 key

WXNXCEHXYPACJF-SSDOTTSWSA-N

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.

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)

Certificates of Analysis (COA)

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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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