Chiral Discrimination Effects in Langmuir Monolayers:  Monolayers of Palmitoyl Aspartic Acid,N-Stearoyl Serine Methyl Ester, andN-Tetradecyl-γ,δ-dihydroxypentanoic Acid Amide

2003 ◽  
Vol 107 (15) ◽  
pp. 3464-3475 ◽  
Author(s):  
N. Nandi ◽  
D. Vollhardt
Keyword(s):  
Methyl Ester ◽  
Aspartic Acid ◽  
Acid Amide ◽  
Langmuir Monolayers ◽  
Chiral Discrimination

Chiral discrimination in Langmuir monolayers of N-eicosanoylproline methyl ester

1995 ◽  
Vol 75 (2) ◽  
pp. 163-169 ◽  
Author(s):  
Jack Y.-J. Uang ◽  
Dennis P. Parazak ◽  
Keith J. Stine
Keyword(s):  
Methyl Ester ◽  
Langmuir Monolayers ◽  
Chiral Discrimination

scholarly journals An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide

1969 ◽  
Vol 113 (2) ◽  
pp. 377-386 ◽  
Author(s):  
R. S. Bayliss ◽  
J. R. Knowles ◽  
Grith B. Wybrandt
Keyword(s):  
Methyl Ester ◽  
Aspartic Acid ◽  
Active Site ◽  
Irreversible Inhibitor ◽  
Aspartic Acid Residue ◽  
Phenylalanine Methyl Ester

Pepsin reacts stoicheiometrically with the active-site-directed irreversible inhibitor N-diazoacetyl-l-phenylalanine methyl ester, with concomitant loss of all proteolytic and peptidolytic activity. The reagent esterifies a unique aspartic acid residue in pepsin, which is in the sequence:Ile-Val-Asp-Thr-Gly-Thr-Ser

The Inactivation of Penicillopepsin with l,2-Epoxy-3-(p-nitrophenoxy)propane, an Active-Site Directed Reagent

1974 ◽  
Vol 52 (11) ◽  
pp. 1018-1023 ◽  
Author(s):  
G. Mains ◽  
T. Hofmann
Keyword(s):  
Methyl Ester ◽  
Aspartic Acid ◽  
Active Site ◽  
Side Chain ◽  
Porcine Pepsin ◽  
Protein Inactivation ◽  
Pepsin Inhibitor

Penicillopepsin was fully inactivated by the pepsin inhibitor 1,2-epoxy-3-(p-nitrophenoxy) propane, and 1.3 ± 0.3 mol of reagent became associated with each mole of protein. Inactivation was more rapid at pH 3.0 than at pH 6.0. Approximately 1 equivalent of the bound reagent was esterified to an aspartic acid side chain. Enzyme previously inactivated with diazoacetylnorleucine methyl ester did not react with the epoxide; and enzyme that was first inactivated with the epoxide did not react with the diazo inhibitor. The results add further evidence for the enzymatic similarity of porcine pepsin and penicillopepsin.

Chiral Discrimination Effects in Langmuir Monolayers of 1-O-Hexadecyl Glycerol

2004 ◽  
Vol 108 (1) ◽  
pp. 327-335 ◽  
Author(s):  
N. Nandi ◽  
D. Vollhardt ◽  
G. Brezesinski
Keyword(s):  
Langmuir Monolayers ◽  
Chiral Discrimination

Efficient method for the synthesis of fatty acid amide from soybean oil methyl ester catalysed by modified CaO

2013 ◽  
Vol 92 (5) ◽  
pp. 871-875 ◽  
Author(s):  
Jie Zhang ◽  
Dan Cai ◽  
Shanshan Wang ◽  
Ying Tang ◽  
Zhao Zhang ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Methyl Ester ◽  
Soybean Oil ◽  
Efficient Method ◽  
Acid Amide ◽  
Soybean Oil Methyl Ester ◽  
Fatty Acid Amide

scholarly journals An active-site peptide from pepsin C

1971 ◽  
Vol 123 (1) ◽  
pp. 75-82 ◽  
Author(s):  
J. Kay ◽  
A. P. Ryle
Keyword(s):  
Methyl Ester ◽  
Aspartic Acid ◽  
Active Site ◽  
Carboxyl Group ◽  
Active Site Residue ◽  
Aspartic Acid Residue ◽  
Porcine Pepsin ◽  
Ph Values ◽  
Complete Inactivation ◽  
Active Site Sequence

Porcine pepsin C is inactivated rapidly and irreversibly by diazoacetyl-dl-norleucine methyl ester in the presence of cupric ions at pH values above 4.5. The inactivation is specific in that complete inactivation accompanies the incorporation of 1mol of inhibitor residue/mol of enzyme and evidence has been obtained to suggest that the reaction occurs with an active site residue. The site of reaction is the β-carboxyl group of an aspartic acid residue in the sequence Ile-Val-Asp-Thr. This sequence is identical with the active-site sequence in pepsin and the significance of this in terms of the different activities of the two enzymes is discussed.

Chiral discrimination in the dissociation of the intermolecular excimer of N-acetyl-1-pyrenylalanine methyl ester

1987 ◽  
Vol 109 (10) ◽  
pp. 3068-3076 ◽  
Author(s):  
F. Lopez-Arbeloa ◽  
R. Goedeweeck ◽  
F. Ruttens ◽  
F. C. De Schryver ◽  
M. Sisido
Keyword(s):  
Methyl Ester ◽  
Chiral Discrimination

scholarly journals COMPARISON OF L-ASPARAGINE INTERACTIONS WITH PYRIDINE DERIVATIVES, PYRIDOXAL- 5'-PHOSPHATE AND PYRIDOXINE, IN AQUEOUS SOLUTIONS: THERMODYNAMIC ASPECTS

2021 ◽  
Vol 64 (5) ◽  
pp. 12-18
Author(s):  
Elena Yu. Tyunina ◽  
Olga N. Krutova ◽  
Alexandr I. Lytkin
Keyword(s):  
Aqueous Solution ◽  
Aqueous Solutions ◽  
Aspartic Acid ◽  
Acid Amide ◽  
The Body ◽  
Biologically Active ◽  
Stable Complex ◽  
Thermochemical Study ◽  
Oh Groups ◽  
Heat Effects

Interactions of proteins with various biologically active substances (hormones, drugs, enzymes, etc.) underlie many biochemical processes in the body. As part of the long-term task to studying various aspects of the interaction between model protein compounds and heterocyclic compounds that are into the structure of many enzymes and drugs, the thermochemical study of aqueous solutions containing aspartic acid amide (L-asparagine) and peridoxal-5¢-phosphate was carried out. Calorimetric measurements of the enthalpy of L-asparagine dissolution in an aqueous solution with pyridoxal-5¢-phosphate additives were performed on an ampoule-type isoperibolic dissolution calorimeter at 298.15 K. The error of measuring single heat effects was below 0.2%. The relative combined uncertainty in the measurements of the enthalpies of dissolution was not more than 0.7%. Based on the obtained experimental data and the using the HEAT computer program, the binding constants and thermodynamic parameters (lgK, ΔcG, ΔcH, ΔcS) of the complex formation between the reagents under study were calculated. A comparison of the affinity of amino acids to interaction with pyridoxal-5¢-phosphate and pyridoxine was carried out. The features of their behavior in an aqueous solution are revealed. It is shown that the interaction of L-asparagine with pyridoxine leads to the formation of a more stable complex than with peridoxal-5¢-phosphate. This fact may be explained in terms of a bulky phosphate group that hinders apparently the interaction of POP with aspartic acid amide. In addition, the peridoxal-5¢-phosphate molecule contains intramolecular hydrogen bonds between aldehyde CHO and phenolic OH groups, which must be destroyed by the interaction of peridoxal-5' - phosphate with an amino acid, which requires additional energy expenses. Thus, the selectivity of the interaction and the stability of the formed complexes are mainly regulated by the factors of structural and energy complementarity.

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