140480-84-8Relevant articles and documents
Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins
Balti, Rafik,Nedjar-Arroume, Naima,Adje, Estelle Yaba,Guillochon, Didier,Nasri, Moncef
, p. 3840 - 3846 (2010)
The angiotensin I-converting enzyme (ACE) inhibitory activities of protein hydrolysates prepared from cuttlefish (Sepia officinalis) proteins by treatment with various bacterial proteases were investigated. The hydrolysate generated by the crude enzyme from Bacillus mojavensis A21 displayed the highest ACE inhibitory activity, and the higher inhibition activity (87.11 ± 0.92% at 2 mg/mL) was obtained with hydrolysis degree of 16%. This hydrolysate was fractionated by size exclusion chromatography on a Sephadex G-25 into eight major fractions (P1-P8). Fraction P6, which exhibited the highest ACE inhibitory activity, was then fractionated by reversed-phase high performance liquid chromatography (RP-HPLC). Eleven ACE inhibitory peptides were isolated, and their molecular masses and amino acids sequences were determined using ESI-MS and ESI-MS/ MS, respectively. The structures of the most potent peptides were identified as Ala-His-Ser-Tyr, Gly-Asp-Ala-Pro, Ala-Gly-Ser-Pro and Asp-Phe-Gly. The first peptide displayed the highest ACE inhibitory activity with an IC50 of 11.6 μM. The results of this study suggest that cuttlefish protein hydrolysates are a good source of ACE inhibitory peptides.
A Flexible Polyphosphate-Driven Regeneration System for Coenzyme A Dependent Catalysis
Mordhorst, Silja,Maurer, Alice,Popadi?, Désirée,Brech, Johanna,Andexer, Jennifer N.
, p. 4164 - 4168 (2017)
Coenzyme A (CoA) is a common cofactor in biochemical reactions, and CoA-dependent enzymes catalyze essential steps in anabolism and catabolism. This complex molecule also plays an important role in the synthesis of many high-value products, such as synthetic antibiotics, vitamins, pheromones, and biopolymers. Nevertheless, the synthetic potential for biocatalytic processes cannot be fully exploited owing to the lack of an efficient regeneration system. Here, we report an acyl-CoA regeneration system with integrated adenosine triphosphate (ATP) regeneration that is based on inexpensive polyphosphate as the single energy source. In the four-enzyme cascade, two cofactors, acyl-CoA and ATP, are each regenerated up to 2000 times. The applicability for different acyl donors and acceptors is shown by HPLC analysis. Owing to its flexibility toward virtually all relevant substrates, the system has the potential to make CoA-dependent reactions more accessible for chemical synthesis in vitro.
The utilization of alanine, glutamic acid, and serine as amino acid substrates for glycine N-acyltransferase.
van der Westhuizen,Pretorius,Erasmus
, p. 102 - 109 (2000)
The conjugation of benzoyl-CoA with the aliphatic and acidic amino acids by glycine N-acyltransferase, as well as the amides of the latter group, was investigated. Bovine and human liver benzoyl-amino acid conjugation were investigated using electrospray ionization tandem mass spectrometry (ESI-MS-MS). Bovine glycine N-acyltransferase catalyzed conjugation of benzoyl-CoA with Gly (Km(Gly) = 6.2 mM), Asn (Km(Asn) = 129 mM), Gln (Km(Gln) = 353 mM), Ala (Km(Ala) = 1573 mM), Glu (Km(Glu) = 1148 mM) as well as Ser in a sequential mechanism. In the case of the human form, conjugation with Gly (Km(Gly) = 6.4 mM), Ala (Km(Ala) = 997 mM), and Glu was detected. The presence of these alternative conjugates did not inhibit bovine glycine N-acyltransferase activity significantly. Considering the relatively low levels at which these conjugates are formed, it is unlikely that they will have a significant contribution to acyl-amino acid conjugation under normal conditions in vivo. However, their cumulative contribution to acyl-amino acid conjugation under metabolic disease states may prove to have a useful contribution to detoxification of elevated acyl-CoAs.
Effect of alkylamine on activity and stability of immobilized angiotensin converting enzyme
Tian, Qingqing,Zhou, Naiyuan,Zeng, Weixiu,Chen, Yingying,Wu, Shuang,Duan, Wei,Chen, Bo,Yao, Shouzhuo
, p. 16 - 19 (2012)
Angiotensin converting enzyme (ACE) was immobilized on chitosan microspheres with glutaraldehyde as cross-linking reagent. The activity and stability of immobilized ACE (I-ACE) were improved by further modification with alkylamines. The modification conditions were optimized. The characteristics of I-ACE and modified I-ACE (MI-ACE) including activity, kinetic parameters, optimal pH and temperature, stability and reusability were investigated. After modification, I-ACE activity was increased, Km decreased from 4.33 mM to 2.61 mM, optimal pH value was altered, pH stability, storage stability and thermal stability were improved, and optimal temperature did not change.
Enzymatic characterization and elucidation of the catalytic mechanism of a recombinant bovine glycine N-acyltransferase
Badenhorst, Christoffel P. S.,Jooste, Maritza,Van Dijk, Alberdina A.
, p. 346 - 352 (2012)
Glycine conjugation, a phase II detoxification process, is catalyzed by glycine N-acyltransferase (GLYAT; E.C. 2.3.1.13). GLYAT detoxifies various xenobiotics, such as benzoic acid, and endogenous organic acids, such as isovaleric acid, which makes GLYAT important in the management of organic acidemias in humans. We cloned the open reading frame encoding the bovine ortholog of GLYAT from bovine liver mRNA into the bacterial expression vector pColdIII. The recombinant enzyme was expressed, partially purified, and enzymatically characterized. Protein modeling was used to predict Glu 226 of bovine GLYAT to be catalytically important. This was assessed by constructing an E226Q mutant and comparing its enzyme kinetics to that of the wild-type recombinant bovine GLYAT. The Michaelis constants for benzoyl-CoA and glycine were determined and were similar for wild-type recombinant GLYAT, E226Q recombinant GLYAT, and GLYAT present in bovine liver. At pH 8.0, the E226Q mutant GLYAT had decreased activity, which could be compensated for by increasing the reaction pH. This suggested a catalytic mechanism in which Glu226 functions to deprotonate glycine, facilitating nucleophilic attack on the acyl- CoA. The recombinant bovine GLYAT enzyme, combined with this new understanding of its active site and reaction mechanism, could be a powerful tool to investigate the functional significance of GLYAT sequence variations. Eventually, this should facilitate investigations into the impact of known and novel sequence variations in the human GLYAT gene. Copyright
Synthesis and cytotoxicity of novel dispiro derivatives of 5-arylidenoxazolones, potential inhibitors of p53—MDM2 protein-protein interaction
Beloglazkina,Skvortsov,Tafeenko,Majouga,Zyk,Beloglazkina
, p. 562 - 569 (2018)
Regioselective synthesis of new dispiro indolinones combining both an indolinone and an oxazolone fragment in their structure comprised the 1,3-dipolar cycloaddition of azomethine ylides, generated in situ from isatin and sarcosine, at 2-aryl-5-arylmethylidene-substituted 1,3-oxazol-5(4H)-ones. When ortho and para halogen atoms were present in the aromatic substituents of the starting oxazolones, complex mixtures containing large amounts of oxazoline ring opening products and their dispiro derivatives were formed. The cytotoxicity of compounds was tested by MTT on LNCaP, PC3, HCT116, MCF7, A549, HEK, and VA13 cell lines. The compound possessing the best cytotoxicity revealed the IC50 = 1.08±0.96 μM towards the p53- expressing LNCaP cells and lower activity (IC50 = 3.21±1.45 μM) towards the non-expressing p53 protein PC3 cells, however, it has proved inactive towards the HCT cells, both expressing (HCТ+/+) and non-expressing (HCT–/–) p53.
Interactions between Penicillin-Binding Proteins (PBPs) and Two Novel Classes of PBP Inhibitors, Arylalkylidene Rhodanines and Arylalkylidene Iminothiazolidin-4-ones
Zervosen, Astrid,Lu, Wei-Ping,Chen, Zhouliang,White, Ronald E.,Demuth Jr., Thomas P.,Frere, Jean-Marie
, p. 961 - 969 (2004)
Several non-β-lactam compounds were active against various gram-positive and gram-negative bacterial strains. The MICs of arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-ones were lower than those of ampicillin and cefotaxime for methicillin-resistant Staphylococcus aureus MI339 and vancomycin-resistant Enterococcus faecium EF12. Several compounds were found to inhibit the cell wall synthesis of S. aureus and the last two steps of peptidoglycan biosynthesis catalyzed by ether-treated cells of Escherichia coli or cell wall membrane preparations of Bacillus megaterium. The effects of the arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-one derivatives on E. coli PBP 3 and PBP 5, Streptococcus pneumoniae PBP 2xS (PBP 2x from a penicillin-sensitive strain) and PBP 2xR (PBP 2x from a penicillin-resistant strain), low-affinity PBP 2a of S. aureus, and the Actinomadura sp. strain R39 and Streptomyces sp. strain R61 DD-peptidases were studied. Some of the compounds exhibited inhibitory activities in the 10 to 100 μM concentration range. The inhibition of PBP 2xS by several of them appeared to be noncompetitive. The dissociation constant for the best inhibitor (Ki = 10 μM) was not influenced by the presence of the substrate.
Influence of pH of an aqueous-organic solvent on the kinetics of N-acylation of α-amino acids with benzoic acid esters
Kuritsyn,Sadovnikov,Khripkova,Kalinina,Shcherbakova
, p. 45 - 47 (2006)
The pH dependence of the apparent rate constants and activation parameters (enthalpy, entropy) of N-acylation of α-amino acids with benzoic acid esters in water-2-propanol solvent was studied. Pleiades Publishing, Inc. 2006.
Synthesis, assessment and corrosion protection investigations of some novel peptidomimetic cationic surfactants: Empirical and theoretical insights
Abd El-Lateef, Hany M.,Abdrabo, Wessam S.,Elgendy, Bahaa,Soliman, Kamal A.,Tantawy, Ahmed H.
, (2020)
Three novel peptidomimetic cationic surfactants were synthesized in good yields. The chemical configurations of these surfactants were clarified using 1H, 13C NMR and FT-IR spectroscopy. The inhibition capacity and adsorption performance of these compounds on C-steel were studied by electrochemical techniques (Electrochemical impedance spectroscopy (EIS) and Potentiodynamic polarization (PDP) methods). The prepared compounds demonstrated outstanding protection power for the erosion of C-steel in 0.5 M HCl at 323 K. The PDP studies demonstrated that the novel surfactants behaved as mixed-type additives. The protection capacity rises with an increasing surfactant dose, with values ranging from 93.10 to 98.25percent at 100 ppm. The adsorption of additives on the electrode interface follows the Langmuir model and contains chemisorption modes. The Monte Carlo (MD) simulations and density functional theory (DFT) calculations support the experimental findings and provide insight into the understanding of the adsorption features and protection performance mechanisms of the examined surfactants.
Palladium-catalyzed amidocarbonylation - A new, efficient synthesis of N-acyl amino acids
Beller,Eckert,Vollmuller,Bogdanovic,Geissler
, p. 1494 - 1496 (1997)
For the first time palladium catalysts have been used successfully for the amidocarbonylation reaction. The activity of the cobalt catalysts that were used exclusively beforehand has now been exceeded by an order of magnitude, and the reaction can be performed under far milder conditions. Palladium-catalyzed amidocarbonylation reactions can now be used for the synthesis of a much wider range of N-acyl amino acids.
