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A1057

Sigma-Aldrich

L-Aspartic acid β-(7-amido-4-methylcoumarin)

≥98%, suitable for ligand binding assays

Sinónimos:

L-Aspartic acid β-(4-methyl-7-coumarinylamide), L-Aspartic acid 4-(4-methyl-7-coumarinylamide)

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About This Item

Fórmula empírica (notación de Hill):
C14H14N2O5
Número de CAS:
133628-73-6
Peso molecular:
290.27
MDL number:
MFCD00236804
UNSPSC Code:
12352209
PubChem Substance ID:
24890500
NACRES:
NA.26

product name

L-Aspartic acid β-(7-amido-4-methylcoumarin), fluorescent amino acid

Quality Level

200

assay

≥98%

form

powder

technique(s)

ligand binding assay: suitable

color

white to off-white

storage temp.

−20°C

SMILES string

CC1=CC(=O)Oc2cc(NC(=O)C[C@H](N)C(O)=O)ccc12

InChI

1S/C14H14N2O5/c1-7-4-13(18)21-11-5-8(2-3-9(7)11)16-12(17)6-10(15)14(19)20/h2-5,10H,6,15H2,1H3,(H,16,17)(H,19,20)/t10-/m0/s1

InChI key

ARZPQBJTLVVDNP-JTQLQIEISA-N

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Categorías relacionadas

Biochem/physiol Actions

L-Aspartic acid β-(7-amido-4-methylcoumarin) is used as a fluorogenic substrate for studying the specificity and kinetics of lysosomal glycoasparaginase(s) (aspartylglucosaminidase) and L-asparaginase(s).
L-Aspartic acid-β-7-amido-4-methylcoumarin is sensitive and specific fluorogenic substrate used to assay for lysosomal glycoasparaginase (aspartylglucosaminidase) activity and the diagnosis of aspartylglucosaminuria.

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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Voznyi YaV et al.
Journal of inherited metabolic disease, 16(6), 929-934 (1993-01-01)
L-Aspartic acid-beta-7-amido-4-methylcoumarin is a sensitive and specific fluorogenic substrate for lysosomal glycoasparaginase (aspartylglucosaminidase). Fibroblasts and leukocytes from 8 patients with aspartylglucosaminuria, showed 1-7% of the mean normal glycoasparaginase activity. Heterozygotes showed intermediate activities. Glycoasparaginase activity in chorionic villi, cultured trophoblasts
P Ylikangas et al.
Analytical biochemistry, 280(1), 42-45 (2000-05-11)
The antineoplastic enzyme L-asparaginase is commonly used for the induction of remission in acute lymphoblastic leukemia (ALL). There is no simple method available for measuring the activity of this highly toxic drug. We incubated L-asparaginase from Erwinia chrysanthemi with L-aspartic
I Mononen et al.
Clinical chemistry, 40(3), 385-388 (1994-03-01)
Serum, plasma, and lymphocytes from aspartylglycosaminuria (AGU) patients and carriers and from normal controls were incubated with a fluorescent glycosylasparaginase substrate, L-aspartic acid beta-(7-amido-4-methylcoumarin), and the release of 7-amino-4-methylcoumarin was measured fluorometrically after incubation for 1-4 h. The mean glycosylasparaginase
I T Mononen et al.
Analytical biochemistry, 208(2), 372-374 (1993-02-01)
Recent experimental work on the mechanism of action of glycosylasparaginase suggests that the enzyme specifically reacts toward the L-asparagine or L-aspartic acid moiety of its substrates. Based on this, a new sensitive assay for glycosylasparaginase activity has been developed using
Seiji Saito et al.
Biochemical and biophysical research communications, 377(4), 1168-1172 (2008-11-11)
To elucidate the basis of aspartylglucosaminuria (AGU) from the viewpoint of enzyme structure, we constructed structural models of mutant aspartylglucosaminidase (AGA) proteins using molecular modeling software, TINKER. We classified the amino acid substitutions responsible for AGU and divided them into

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