L-Valine β-naphthylamide
Need Assistance?
  • US & Canada:
    +
  • UK: +

L-Valine β-naphthylamide

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category
L-Amino Acids
Catalog number
BAT-005889
CAS number
729-24-8
Molecular Formula
C15H18N2O3S
Molecular Weight
242.32
L-Valine β-naphthylamide
IUPAC Name
(2S)-2-amino-3-methyl-N-naphthalen-2-ylbutanamide
Synonyms
H-Val-βNA
Density
1.2±0.1 g/cm3
Boiling Point
457.9±28.0 °C
Storage
Store at -20°C
InChI
InChI=1S/C15H18N2O/c1-10(2)14(16)15(18)17-13-8-7-11-5-3-4-6-12(11)9-13/h3-10,14H,16H2,1-2H3,(H,17,18)/t14-/m0/s1
InChI Key
OBGGZBHESVNMSA-AWEZNQCLSA-N
Canonical SMILES
CC(C)C(C(=O)NC1=CC2=CC=CC=C2C=C1)N
1. Comparative studies of two cathepsin B isozymes from porcine spleen. Isolation, polypeptide chain arrangements, and enzyme specificity
T Takahashi, S Yonezawa, A H Dehdarani, J Tang J Biol Chem. 1986 Jul 15;261(20):9368-74.
Our previous studies on carbohydrate structures of purified porcine spleen cathepsin B indicated that there are two cathepsin B isozymes, each containing a different carbohydrate (Takahashi, T., Schmidt, P.G., and Tang, J. (1984) J. Biol. Chem. 259, 6059-6062). We have now isolated these two enzymes and carried out a comparative study on their structures and enzymic properties. The major isozyme (CB-I) is a two-chain enzyme (Mr = 28,000) with a light chain (Mr = 5,000) and a heavy chain (Mr = 23,000), whereas the minor enzyme (CB-II) is a single chain enzyme (Mr = 27,000). The NH2-terminal amino acid residues of CB-I were leucine and valine for the light and heavy chain, respectively. However, the NH2-terminal residue of CB-II was not available for automated Edman degradation. In addition, peptide mapping experiments indicated a difference in the primary structure of these two proteins. Despite such structural differences, they are similar in many enzymic properties. CB-I was more catalytically efficient than CB-II toward synthetic substrates, except for the substrate benzoyl-L-arginine beta-naphthylamide for which the relative catalytic efficiency is reversed. Both isozymes degraded glucagon by a dipeptidyl carboxypeptidase activity. Under the same conditions, CB-I was 4-5 times more efficient than CB-II. The results indicate that the cathepsin B isozymes are two separate gene products, but they are similar in enzymic properties.
2. Peptidase-deficient mutants of Escherichia coli
C G Miller, G Schwartz J Bacteriol. 1978 Aug;135(2):603-11. doi: 10.1128/jb.135.2.603-611.1978.
Mutant derivatives of Escherichia coli K-12 deficient in several peptidases have been obtained. Mutants lacking a naphthylamidase, peptidase N, were isolated by screening for colonies unable to hydrolyze L-alanine beta-naphthylamide. Other mutants were isolated using positive selections for resistance to valine peptides. Mutants lacking peptidase A, a broad-specificity aminopeptidase, were obtained by selection for resistance to L-valyl-L-leucine amide. Mutants lacking a dipeptidase, peptidase D, were isolated from a pepN pepA strain by selection for resistance to L-valyl-glycine. Starting with a pepN pepA pepD strain, selection for resistance to L-valyl-glycyl-glycine or several other valine peptides produced mutants deficient in another aminopeptidase, peptidase B. Mutants resistant to L-valyl-L-proline lack peptidase Q, an activity capable of rapid hydrolysis of X-proline dipeptides. Using these selection procedures, a strain (CM89) lacking five different peptidases has been isolated. Although still sensitive to valine, this strain is resistant to a variety of valine di- and tripeptides. The ability of this strain to use peptides as sources of amino acids is much more restricted than that of wild-type E. coli strains. Strains containing only one of the five peptidases missing in CM89 have been constructed by transduction. The peptide utilization profiles of these strains show that each of the five peptidases can function during growth in the catabolism of peptides.
3. Leucine Aminopeptidase in Eggs of the Soybean Cyst Nematode Heterodera glycines
P M Tefft, L W Bone J Nematol. 1985 Jul;17(3):270-4.
Supernatant from a sonicated macerate of eggs of Heterodera glycines hydrolyzed L-leucine beta-naphthylamide and L-leucine 7-amido-4-methylcoumarin. Rate of substrate hydrolysis was influenced by pH and increased with the duration of incubation. A Michaelis-Menten constant of 0.15 mM was obtained. Rate of substrate hydrolysis was decreased by freezing egg supernatant for 26 days or heating above 60 C for 5 minutes. When egg supernatant was incubated with six different substrates, L-leucine beta-naphthylamide was hydrolyzed most readily and L-valine beta-naphthylamide the least readily. The rate of substrate hydrolysis by egg supernatant was not increased by pretreatment of eggs with 3 mM zinc chloride for up to 14 days.
Online Inquiry
Verification code
Inquiry Basket