L-Aspartic acid β-naphthylamide
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L-Aspartic acid β-naphthylamide

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Category
L-Amino Acids
Catalog number
BAT-004121
CAS number
635-91-6
Molecular Formula
C14H14N2O3
Molecular Weight
258.30
L-Aspartic acid β-naphthylamide
IUPAC Name
(3S)-3-amino-4-(naphthalen-2-ylamino)-4-oxobutanoic acid
Synonyms
L-Asp-βNA; H-Asp-bNA; L-ASPARTIC ACID A-(B-NAPHTHYLAMIDE); L-ASPARTYL-B-NAPHTHYLAMIDE
Appearance
White powder
Purity
≥ 98% (TLC)
Density
1.371±0.06 g/cm3
Boiling Point
567.8±45.0 °C
Storage
Store at 2-8 °C
InChI
InChI=1S/C14H14N2O3/c15-12(8-13(17)18)14(19)16-11-6-5-9-3-1-2-4-10(9)7-11/h1-7,12H,8,15H2,(H,16,19)(H,17,18)/t12-/m0/s1
InChI Key
YRMVHTZHFWHHIU-LBPRGKRZSA-N
Canonical SMILES
C1=CC=C2C=C(C=CC2=C1)NC(=O)C(CC(=O)O)N
1. A comparison of peptidase activities and peptide metabolism in cultured mouse keratinocytes and neonatal mouse epidermis
P K Shah, R T Borchardt Pharm Res. 1991 Jan;8(1):70-5. doi: 10.1023/a:1015882323677.
One of the barriers to transdermal delivery of peptides is the metabolic activity of the epidermis. To define this metabolic activity, aminopeptidase activity and Leu-enkephalin metabolism were measured in the epidermis obtained from neonatal mouse skin and in cultured mouse keratinocytes. Aminopeptidase activity was measured fluorometrically using leucine, tyrosine, lysine, and aspartic acid derivatives of beta-naphthylamine as substrates. Similarities in substrate kinetic values (Km and Vmax) and substrate specificity of the enzyme(s) in homogenates prepared from neonatal mouse skin epidermis and cultured mouse keratinocytes strongly suggest that the keratinocytes in culture express the same aminopeptidase(s) with the same relative activity as in neonatal skin. The Km and Vmax values for aminopeptidase(s) with different substrates in epidermis homogenates are as follows: leucine beta-naphthylamide (11 microM and 38 nmol.min-1.mg-1), tyrosine beta-naphthylamide (21 microM and 18 nmol.min-1.mg-1), and lysine beta-naphthylamide (11 microM and 35 nmol.min-1.mg-1). Aspartic acid beta-naphthylamide and glutamic acid beta-naphthylamide were not hydrolyzed by these homogenates at pH 7.4 (37 degrees C). Leu-enkephalin hydrolysis by the homogenates from cultured mouse keratinocytes and neonatal mouse epidermis gave similar Km (32 and 24 microM). Vmax (9.77 and 7.55 nmol.min-1.mg-1) and Ki (223 and 194 microM) values. In addition, the cellular homogenates gave similar metabolite profiles for Leu-enkephalin.
2. Aminopeptidases of Bacillus subtilis
E P Desmond, W L Starnes, F J Behal J Bacteriol. 1975 Oct;124(1):353-63. doi: 10.1128/jb.124.1.353-363.1975.
Three enzymes with L- and one enzyme with D-aminopeptidase (EC 3.4.11; alpha-aminoacyl peptide hydrolase) activity have been separated from each other and partially purified from Bacillus subtilis 168 W.T., distinguished with respect to their molecular weights and catalytic properties, and studied in relation to the physiology of this bacterium. One L-aminopeptidase, designated aminopeptidase I, has a molecular weight of 210,000 +/- 20,000, is produced early in growth, and hydrolyzes L-alanyl-beta-naphthylamide most rapidly. Another, designated aminopeptidase II, molecular weight 67,000 +/- 10,000, is also produced early in growth and hydrolyzes L-lysyl-beta-naphthylamide most rapidly. A third, aminopeptidase III, molecular weight 228,000 +/- 20,000, is produced predominantly in early stationary phase and most efficiently utilizes L-alpha-aspartyl-beta-naphthylamide as substrate. The synthesis of aminopeptidase III in early stationary phase suggests that selective catabolism of peptides occurs at this time, perhaps related to the cessation of growth or the onset of early sporulation-associated events. A D-aminopeptidase which hydrolyzes the carboxyl-blocked dipeptide D-alanyl-D-alanyl-beta-naphthylamide (as well as D-alanyl-beta-naphthylamide and D-alanyl-D-alanyl-D-alanine) has also been identified, separated from aminopeptidase II, and purified 170-fold. D-Aminopeptidase, molecular weight 220,000 +/- 20,000, is localized predominantly in the cell wall and periplasm of the organism. This evidence and the variation of the activity during the growth cycle suggest an important function in cell wall or peptide antibiotic metabolism.
3. Variable distribution of aminopeptidase A in male reproductive organs of mammals
Y Agrawal, T Vanha-Perttula Int J Androl. 1985 Jun;8(3):243-56. doi: 10.1111/j.1365-2605.1985.tb00839.x.
Aminopeptidase A (AP-A) was analysed in the reproductive organs of the boar, bull, gerbil and man. High hydrolysis of alpha-L-glutamyl-beta-naphthylamide (GluNA) and alpha-L-aspartyl-beta-naphthylamide (AspNA) with activation by alkaline earth metals was detected in the ampulla, seminal vesicles, and seminal vesicle secretions of the bull and in the cauda epididymis of the boar and gerbil. In man, weak AP-A activity was found in all reproductive tissues. Histochemically, AP-A was localized in the epithelial cells of tissues having a high specific activity for the enzyme. AP-A was absent from human seminal fluid, whilst bovine seminal fluid had strong, and boar seminal fluid weaker, AP-A activity. Gel filtration of bull seminal vesicle secretions and seminal fluid, boar seminal fluid or an homogenate of boar and gerbil epididymal cauda and human epididymis and seminal vesicles on Sephacryl S-300 resulted in a major high-molecular-weight activity peak A at Ve/Vo = 1.17 and another low-molecular-weight peak B at Ve/Vo = 1.51 (man), 1.62 (boar, bull) or 1.75 (gerbil). This fractionation was not in all cases able to separate AP-A from aminopeptidase(s), which were active on L-alanine-beta-naphthylamide (AlaNA) but showed no activation by alkaline earth metals. Homogenates of bovine epididymis showed only the low-molecular-weight GluNA peak B, but two areas of activity for AlaNA hydrolysis. In bovine seminal vesicles and porcine epididymis, AP-A activity appeared to be linked with the functional maturity of these organs. The high-molecular-weight AP-A (peak A) appeared to be the predominant form in seminal fluid.
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