Molecular Mechanism of Physical Gelation of Hydrocarbons by Fatty Acid Amides of Natural Amino Acids.

ChemInform ◽  
2007 ◽  
Vol 38 (39) ◽  
Author(s):  
Asish Pal ◽  
Yamuna K. Ghosh ◽  
Santanu Bhattacharya
Keyword(s):  
Amino Acids ◽  
Fatty Acid ◽  
Molecular Mechanism ◽  
Fatty Acid Amides ◽  
Physical Gelation ◽  
Natural Amino Acids

scholarly journals The Biosynthesis and Metabolism of the N-Acylated Aromatic Amino Acids: N-Acylphenylalanine, N-Acyltyrosine, N-Acyltryptophan, and N-Acylhistidine

2022 ◽  
Vol 8 ◽  
Author(s):  
Suzeeta Bhandari ◽  
Kirpal S. Bisht ◽  
David J. Merkler
Keyword(s):  
Amino Acids ◽  
Fatty Acid ◽  
Acid Amide ◽  
Aromatic Amino Acids ◽  
Amide Bond ◽  
Future Research ◽  
Cellular Functions ◽  
Fatty Acid Amides ◽  
Biological Source ◽  
Fatty Acid Amide

The fatty acid amides are a family of lipids composed of two chemical moieties, a fatty acid and a biogenic amine linked together in an amide bond. This lipid family is structurally related to the endocannabinoid anandamide (N-arachidonoylethanolamine) and, thus, is frequently referred to as a family of endocannabinoid-related lipids. The fatty acid amide family is divided into different classes based on the conjugate amine; anandamide being a member of the N-acylethanolamine class (NAE). Another class within the fatty acid amide family is the N-acyl amino acids (NA-AAs). The focus of this review is a sub-class of the NA-AAs, the N-acyl aromatic amino acids (NA-ArAAs). The NA-ArAAs are not broadly recognized, even by those interested in the endocannabinoids and endocannabinoid-related lipids. Herein, the NA-ArAAs that have been identified from a biological source will be highlighted and pathways for their biosynthesis, degradation, enzymatic modification, and transport will be presented. Also, information about the cellular functions of the NA-ArAAs will be placed in context with the data regarding the identification and metabolism of these N-acylated amino acids. A review of the current state-of-knowledge about the NA-ArAAs is to stimulate future research about this underappreciated sub-class of the fatty acid amide family.

scholarly journals Both Determinants of Allosteric and Active Sites Responsible for Catalytic Activity of Delta 12 Fatty Acid Desaturase by Domain Swapping

2019 ◽  
Author(s):  
Haisu Shi ◽  
Jinlong Tian ◽  
Chen Wu ◽  
Mo Li ◽  
Feiyu An ◽  
...  
Keyword(s):  
Amino Acids ◽  
Catalytic Activity ◽  
Fatty Acid ◽  
Amino Acid ◽  
Molecular Mechanism ◽  
Active Sites ◽  
Transmembrane Domain ◽  
Fatty Acid Desaturase ◽  
Domain Swapping ◽  
The Third

AbstractCheese lacks essential fatty acids (EFAs). Delta 12 fatty acid desaturase (FADS12) is a critical enzyme required for EFA biosynthesis in fermentation of the predominant strains of cheese. Previously, we identified the FADS12 gene and characterized its function for the first time in Geotrichum candidum, a dominant strain used to manufacture soft cheese with white rind. In this study, we analyzed the molecular mechanism of FADS12 function by swapping domains from Mortierella alpina and G. candidum that had, respectively, high and low oleic acid conversion rates. The results revealed three regions that are essential to this process, including regions from the end of the second transmembrane domain to the beginning of the third transmembrane domain, from the end of the third transmembrane domain to the beginning of the fourth transmembrane domain, and from the 30-amino acid from the end of the sixth transmembrane domain to the C-terminal end region. Based on our domain swapping analyses, nine pairs of amino acids including H112, S118, H156, Q161, K301, R306, E307, A309 and S323 in MaFADS12 (K123, A129, N167, M172, T302, D307, I308, E310 and D324 in GcFADS12) were identified as having a significantly effect on FADS12 catalytic efficiency, and linoleic acid and its analogues (12,13-cyclopropenoid fatty acid) were found to inhibit the catalytic activity of FADS12 and related recombinant enzymes. Furthermore, the molecular mechanism of FADS12 inhibition was analyzed. The results revealed two allosteric domains, including one domain from the N-terminal region to the beginning of the first transmembrane domain and another from the 31st amino acid from the end of the sixth transmembrane domain to the C terminus. Y4 and F398 amino acid residues from MaFADS12 and eight pairs of amino acids including G56, L60, L344, G10, Q13, S24, K326 and L344 in MaFADS12 (while Y66, F70, F345, F20, Y23, Y34, F327 and F345 in GcFADS12) played a pivotal role in FADS12 inhibition. Finally, we found that both allosteric and active sites were responsible for the catalytic activity of FADS12 at various temperatures, pH, and times. This study offers a solid theoretical basis to develop preconditioning methods to increase the rate at which GcFADS12 converts oleic and linoleic acids to produce higher levels of EFAs in cheese.

A new method for quantifying the blocking of coated paperboard

TAPPI Journal ◽  
2010 ◽  
Vol 9 (5) ◽  
pp. 29-35 ◽  
Author(s):  
PAULINE SKILLINGTON ◽  
YOLANDE R. SCHOEMAN ◽  
VALESKA CLOETE ◽  
PATRICE C. HARTMANN
Keyword(s):  
Surface Roughness ◽  
Fatty Acid ◽  
Surface Energy ◽  
Film Thickness ◽  
External Factors ◽  
Additive Concentration ◽  
Pressure Surface ◽  
Fatty Acid Amides ◽  
Coated Surfaces ◽  
Definite Period

Blocking is undesired adhesion between two surfaces when subjected to pressure and temperature constraints. Blocking between two coated paperboards in contact with each other may be caused by inter-diffusion, adsorption, or electrostatic forces occurring between the respective coating surfaces. These interactions are influenced by factors such as the temperature, pressure, surface roughness, and surface energy. Blocking potentially can be reduced by adjusting these factors, or by using antiblocking additives such as talc, amorphous silica, fatty acid amides, or polymeric waxes. We developed a method of quantifying blocking using a rheometer. Coated surfaces were put in contact with each other with controlled pressure and temperature for a definite period. We then measured the work necessary to pull the two surfaces apart. This was a reproducible way to accurately quantify blocking. The method was applied to determine the effect external factors have on the blocking tendency of coated paperboards, i.e., antiblocking additive concentration, film thickness, temperature, and humidity.

Synthesis and characteristics of ethylenediamine-N,N'-di-S-α-isovalerate and isomers of its cobalt(III) complexes

1982 ◽  
Vol 47 (1) ◽  
pp. 210-216 ◽  
Author(s):  
Milan Strašák ◽  
František Bachratý ◽  
Jaroslav Majer
Keyword(s):  
Amino Acids ◽  
Absolute Configuration ◽  
Electronic Absorption ◽  
Electronic Absorption Spectra ◽  
Chemical Parameters ◽  
Methyl Group ◽  
Nmr Data ◽  
Physico Chemical ◽  
Natural Amino Acids ◽  
C Nmr

The synthesis and physico-chemical parameters are described of a new complexone based on natural amino acids, viz. ethylenediamine-N,N'-di-S-α-isovalerate (SS-EDDIV). 1H- and 13C-NMR data revealed that the methyl group in the substance are not equivalent. The isomers of the cobalt(III) complex with the asymmetric tetradentate SS-EDDIV ligand were prepared and separated; their characteristics are given. The absolute configuration of two of the five theoretically feasible isomers was determined based on their electronic absorption spectra and circular dichroism data.

Sign in / Sign up

Export Citation Format

Share Document