Disease relevance of Ala-4-nitroanilide

• Escherichia coli K-12 strains contain a cytoplasmic activity, peptidase N, capable of hydrolyzing alanine-p-nitroanilide [1].
• Lysis by KOH and hydrolysis of L-alanine-4-nitroanilide were compared with the Gram reaction of aerobic, microaerophilic, and anaerobic bacteria [2].

High impact information on Ala-4-nitroanilide

• L-alanine-4-nitroanilide as a substrate for microsomal aminopeptidase [3].
• As final concentrations, 50 mmol/L tris(hydroxymethyl)aminomethane x HCl buffer, pH 7.8, and 2 mmol/L alanine-4-nitroanilide are proposed [4].
• Furthermore, peptidase activity was detected in these cell preparations by an assay based on the hydrolysis of alanine-p-nitroanilide into p-nitroaniline and alanine [5].
• In X. laevis oocytes, transport of Ala-4-nitroanilide, Ala-7-amido-4-methylcoumarin, Ala-4-methylanilide and Ala-anilide was associated with transfer of positive charge and the currents were saturable with respect to substrate concentration (K0.5 values: 0.1, 0.2, 0.8 and 3.1 mM, respectively) [6].
• We examined the presence of cell surface aminopeptidase on cultured porcine granulosa cells by employing the aminopeptidase assay using alanine-p-nitroanilide and histochemical staining using L-leucyl-beta-naphthylamide [7].

Anatomical context of Ala-4-nitroanilide

• Purified leukotriene A4 hydrolase from human leukocytes is shown to exhibit peptidase activity towards the synthetic substrates alanine-4-nitroanilide and leucine-4-nitroanilide [8].

Associations of Ala-4-nitroanilide with other chemical compounds

• Once activated, the polysaccharide was reactive with a model substrate, L-alanine-4-nitroanilide, over a pH range of 6-10 [9].
• The purified enzyme cleaved the substrate at the bond between succinyl dialanine and alanine-4-nitroanilide and showed a Km value of 2.1 mM at the optimal pH of 8 [10].

Gene context of Ala-4-nitroanilide

• Aminopeptidase activities were detected in extracts of the free-living nematodes Caenorhabditis elegans and Panagrellus redivivus using the aminoacyl substrate L-alanine-4-nitroanilide [11].
• This activity, hydrolysing leucine-p-nitroanilide and alanine-p-nitroanilide at pH 7.4 was immunoprecipitated by various infected rat and human sera [12].

References