scholarly journals Biochemical and structural exploration of the catalytic capacity of Sulfolobus KDG aldolases

2007 ◽  
Vol 403 (3) ◽  
pp. 421-430 ◽  
Author(s):  
Suzanne Wolterink-van Loo ◽  
André van Eerde ◽  
Marco A. J. Siemerink ◽  
Jasper Akerboom ◽  
Bauke W. Dijkstra ◽  
...  
Keyword(s):  
Biochemical Properties ◽  
Binding Motif ◽  
Phosphate Binding ◽  
Sulfolobus Tokodaii ◽  
Acceptor Substrate ◽  
Hydrogen Bonding Interactions ◽  
Potential Applications ◽  
Multiple Hydrogen Bonding ◽  
Multiple Conformations ◽  
Catalytic Capacity

Aldolases are enzymes with potential applications in biosynthesis, depending on their activity, specificity and stability. In the present study, the genomes of Sulfolobus species were screened for aldolases. Two new KDGA [2-keto-3-deoxygluconate (2-oxo-3-deoxygluconate) aldolases] from Sulfolobus acidocaldarius and Sulfolobus tokodaii were identified, overexpressed in Escherichia coli and characterized. Both enzymes were found to have biochemical properties similar to the previously characterized S. solfataricus KDGA, including the condensation of pyruvate and either D,L-glyceraldehyde or D,L-glyceraldehyde 3-phosphate. The crystal structure of S. acidocaldarius KDGA revealed the presence of a novel phosphate-binding motif that allows the formation of multiple hydrogen-bonding interactions with the acceptor substrate, and enables high activity with glyceraldehyde 3-phosphate. Activity analyses with unnatural substrates revealed that these three KDGAs readily accept aldehydes with two to four carbon atoms, and that even aldoses with five carbon atoms are accepted to some extent. Water-mediated interactions permit binding of substrates in multiple conformations in the spacious hydrophilic binding site, and correlate with the observed broad substrate specificity.

Synthesis and biochemical properties of the novel, enzymatically stable mRNA cap analogues with versatile potential applications

2005 ◽  
Author(s):  
Marcin Kalek ◽  
Jacek Jemielity ◽  
Ewa Grudzien ◽  
Joanna Zuberek ◽  
Zbigniew M. Darzynkiewicz ◽  
...  
Keyword(s):  
Biochemical Properties ◽  
The Novel ◽  
Potential Applications

Exclusive Recognition of Acetone in a Luminescent BioMOF through Multiple Hydrogen-Bonding Interactions

2019 ◽  
Vol 58 (12) ◽  
pp. 7667-7671 ◽  
Author(s):  
Yong-Liang Huang ◽  
Pei-Li Qiu ◽  
Jian-Ping Bai ◽  
Dong Luo ◽  
Weigang Lu ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Hydrogen Bonding Interactions ◽  
Multiple Hydrogen Bonding

Compatibilization of Polypropylene/Corn Starch Plasticized with Diethanol Amine

2012 ◽  
Vol 610-613 ◽  
pp. 475-479
Author(s):  
Jia Hao Qiu ◽  
Pin Gan Song ◽  
Shen Yuan Fu ◽  
Xian Xun Ge ◽  
Bing Huang ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Corn Starch ◽  
Intermolecular Hydrogen Bonding ◽  
Starch Granules ◽  
Reactive Compatibilization ◽  
Hydrogen Bonding Interactions ◽  
Potential Applications ◽  
Plasticized Starch ◽  
Reduction Effect

In the presented paper, diethanol amine is employed to plasticize corn starch, and plasticized starch is incorporated into polypropylene to create semibio-based composites with the aid of compatibilizer, maleic anhydride-grafted PP (PPMA). Compared with PP/starch blend, the presence of diethanol amine changes the morphology and increases the plasticity of starch due to the reduction effect of intermolecular hydrogen bonding interactions. Adding PPMA could reduce the dispersed size of starch granules in the polymer matrix due to in situ reactive compatibilization. Addition of 30 wt% PPMA decreases the starch granules size from ~10 μm to ~5 μm, and increases the tensile strength from 16 MPa for PP/plasticized starch to 30 MPa, increased by 87.5%. Thus, as-created bio-composites with improved mechanical properties will find many potential applications such as packaging.

scholarly journals Complexation of 2,6-helic[6]arene and its derivatives with 1,1′-dimethyl-4,4′-bipyridinium salts and protonated 4,4'-bipyridinium salts: an acid–base controllable complexation

2019 ◽  
Vol 15 ◽  
pp. 1795-1804 ◽  
Author(s):  
Jing Li ◽  
Qiang Shi ◽  
Ying Han ◽  
Chuan-Feng Chen
Keyword(s):  
Association Constants ◽  
The Other ◽  
Acid Base ◽  
Polar Solvents ◽  
X Ray ◽  
H Nmr ◽  
Hydrogen Bonding Interactions ◽  
Acids And Bases ◽  
Multiple Hydrogen Bonding ◽  
Nmr Titrations

2,6-Helic[6]arene and its derivatives were synthesized, and their complexation with 1,1′-dimethyl-4,4′-bipyridinium and protonated 4,4'-bipyridinium salts were investigated in detail. It was found that the helic[6]arene and its derivatives could all form 1:1 complexes with both 1,1′-dimethyl-4,4'-bipyridinium salts and protonated 4,4'-bipyridinium salts in solution and in the solid state. Especially, the helic[6]arene and its derivatives containing 2-hydroxyethoxy or 2-methoxyethoxy groups exhibited stronger complexation with the guests than the other helic[6]arene derivatives for the additional multiple hydrogen bonding interactions between the hosts and the guests, which were evidenced by 1H NMR titrations, X-ray crystal structures and DFT calculations. Moreover, it was also found that the association constants (K a) of the complexes could be significantly enhanced with larger counteranions of the guests and in less polar solvents. Furthermore, the switchable complexation between the helic[6]arene and protonated 4,4'-bipyridinium salt could be efficiently controlled by acids and bases.

scholarly journals Biochemical Properties and Potential Applications of Recombinant Leucine Aminopeptidase from Bacillus kaustophilus CCRC 11223

2011 ◽  
Vol 12 (11) ◽  
pp. 7609-7625 ◽  
Author(s):  
Yanfei Shen ◽  
Fanghua Wang ◽  
Dongming Lan ◽  
Yuanyuan Liu ◽  
Bo Yang ◽  
...  
Keyword(s):  
Leucine Aminopeptidase ◽  
Biochemical Properties ◽  
Bacillus Kaustophilus ◽  
Potential Applications

scholarly journals Structure-based design, synthesis, and evaluation of the biological activity of novel phosphoroorganic small molecule IAP antagonists

2020 ◽  
Vol 38 (5) ◽  
pp. 1350-1364 ◽  
Author(s):  
Agnieszka Łupicka-Słowik ◽  
Mateusz Psurski ◽  
Renata Grzywa ◽  
Monika Cuprych ◽  
Jarosław Ciekot ◽  
...  
Keyword(s):  
Cancer Cell Line ◽  
Biochemical Properties ◽  
Inhibitor Of Apoptosis ◽  
Binding Motif ◽  
Inhibitory Influence ◽  
Design Synthesis ◽  
Inhibitor Of Apoptosis Protein ◽  
Design And Synthesis ◽  
Apoptosis Protein ◽  
Fluorescence Polarization Assay

Summary One of the strategies employed by novel anticancer therapies is to put the process of apoptosis back on track by blocking the interaction between inhibitor of apoptosis proteins (IAPs) and caspases. The activity of caspases is modulated by the caspases themselves in a caspase/procaspase proteolytic cascade and by their interaction with IAPs. Caspases can be released from the inhibitory influence of IAPs by proapoptotic proteins such as secondary mitochondrial activator of caspases (Smac) that share an IAP binding motif (IBM). The main purpose of the present study was the design and synthesis of phosphorus-based peptidyl antagonists of IAPs that mimic the endogenous Smac protein, which blocks the interaction between IAPs and caspases. Based on the structure of the IAP antagonist and recently reported thiadiazole derivatives, we designed and evaluated the biochemical properties of a series of phosphonic peptides bearing the N-Me-Ala-Val/Chg-Pro-OH motif (Chg: cyclohexylglycine). The ability of the obtained compounds to interact with the binding groove of the X-linked inhibitor of apoptosis protein baculovirus inhibitor of apoptosis protein repeat (XIAP BIR3) domain was examined by a fluorescence polarization assay, while their potential to induce autoubiquitination followed by proteasomal degradation of cellular IAP1 was examined using the MDA-MB-231 breast cancer cell line. The highest potency against BIR3 was observed among peptides containing C-terminal phosphonic phenylalanine analogs, which displayed nanomolar Ki values. Their antiproliferative potential as well as their proapoptotic action, manifested by an increase in caspase-3 activity, was examined using various cell lines.

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