A4375
N-Acetyl-D-alanine
≥98% (TLC), suitable for ligand binding assays
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About This Item
Produtos recomendados
product name
N-Acetyl-D-alanine,
Ensaio
≥98% (TLC)
Nível de qualidade
forma
powder
técnica(s)
ligand binding assay: suitable
cor
white to off-white
temperatura de armazenamento
−20°C
cadeia de caracteres SMILES
C[C@@H](NC(C)=O)C(O)=O
InChI
1S/C5H9NO3/c1-3(5(8)9)6-4(2)7/h3H,1-2H3,(H,6,7)(H,8,9)/t3-/m1/s1
chave InChI
KTHDTJVBEPMMGL-GSVOUGTGSA-N
Ações bioquímicas/fisiológicas
N-Acetyl-D-alanine may be used with other D-aminoacylated amino acids as a substrate for the identification, differentiation and characterization of D-aminoacylase(s)/amidohydrolase(s). N-acetyl-D-alanine may be used to study aglycon pocket specific binding on vancomycin.
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Certificados de análise (COA)
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Chemistry & biology, 5(5), 293-298 (1998-05-14)
Vancomycin and related glycopeptide antibiotics exert their antimicrobial effect by binding to carboxy-terminal peptide targets in the bacterial cell wall and preventing the biosynthesis of peptidoglycan. Bacteria can resist the action of these agents by replacing the peptide targets with
Journal of chromatographic science, 40(2), 83-86 (2002-03-08)
The analysis of the binding data of D,L-dansyl amino acids on a vancomycin stationary phase is investigated in relation to the addition of N-acetyl-D-alanine in the mobile phase. This eluent additive acts as a specific competing agent for the aglycone
Journal of molecular biology, 385(5), 1422-1432 (2008-11-04)
The crystal structures of three vancomycin complexes with two vancomycin-sensitive cell-wall precursor analogs (diacetyl-Lys-D-Ala-D-Ala and acetyl-D-Ala-D-Ala) and a vancomycin-resistant cell-wall precursor analog (diacetyl-Lys-D-Ala-D-lactate) were determined at atomic resolutions of 1.80 A, 1.07 A, and 0.93 A, respectively. These structures not
Bioorganic & medicinal chemistry, 16(23), 10061-10074 (2008-10-28)
Peptidyl alpha-hydroxylating monooxygenase (PHM) functions in vivo towards the biosynthesis of alpha-amidated peptide hormones in mammals and insects. PHM is a potential target for the development of inhibitors as drugs for the treatment of human disease and as insecticides for
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