Mazur A

References (8)

Title : The tetrameric structure of the novel haloalkane dehalogenase DpaA from Paraglaciecola agarilytica NO2 - Mazur_2021_Acta.Crystallogr.D.Struct.Biol_77_347
Author(s) : Mazur A , Prudnikova T , Grinkevich P , Mesters JR , Mrazova D , Chaloupkova R , Damborsky J , Kuty M , Kolenko P , Kuta Smatanova I
Ref : Acta Crystallographica D Struct Biol , 77 :347 , 2021
Abstract : Haloalkane dehalogenases (EC are microbial enzymes that catalyse the hydrolytic conversion of halogenated compounds, resulting in a halide ion, a proton and an alcohol. These enzymes are used in industrial biocatalysis, bioremediation and biosensing of environmental pollutants or for molecular tagging in cell biology. The novel haloalkane dehalogenase DpaA described here was isolated from the psychrophilic and halophilic bacterium Paraglaciecola agarilytica NO2, which was found in marine sediment collected from the East Sea near Korea. Gel-filtration experiments and size-exclusion chromatography provided information about the dimeric composition of the enzyme in solution. The DpaA enzyme was crystallized using the sitting-drop vapour-diffusion method, yielding rod-like crystals that diffracted X-rays to 2.0A resolution. Diffraction data analysis revealed a case of merohedral twinning, and subsequent structure modelling and refinement resulted in a tetrameric model of DpaA, highlighting an uncommon multimeric nature for a protein belonging to haloalkane dehalogenase subfamily I.
ESTHER : Mazur_2021_Acta.Crystallogr.D.Struct.Biol_77_347
PubMedSearch : Mazur_2021_Acta.Crystallogr.D.Struct.Biol_77_347
PubMedID: 33645538
Gene_locus related to this paper: 9alte-k6xnl5

Title : Structural Analysis of the Ancestral Haloalkane Dehalogenase AncLinB-DmbA - Mazur_2021_Int.J.Mol.Sci_22_11992
Author(s) : Mazur A , Grinkevich P , Chaloupkova R , Havlickova P , Kascakova B , Kuty M , Damborsky J , Kuta Smatanova I , Prudnikova T
Ref : Int J Mol Sci , 22 : , 2021
Abstract : Haloalkane dehalogenases (EC play an important role in hydrolytic degradation of halogenated compounds, resulting in a halide ion, a proton, and an alcohol. They are used in biocatalysis, bioremediation, and biosensing of environmental pollutants and also for molecular tagging in cell biology. The method of ancestral sequence reconstruction leads to prediction of sequences of ancestral enzymes allowing their experimental characterization. Based on the sequences of modern haloalkane dehalogenases from the subfamily II, the most common ancestor of thoroughly characterized enzymes LinB from Sphingobium japonicum UT26 and DmbA from Mycobacterium bovis 5033/66 was in silico predicted, recombinantly produced and structurally characterized. The ancestral enzyme AncLinB-DmbA was crystallized using the sitting-drop vapor-diffusion method, yielding rod-like crystals that diffracted X-rays to 1.5 A resolution. Structural comparison of AncLinB-DmbA with their closely related descendants LinB and DmbA revealed some differences in overall structure and tunnel architecture. Newly prepared AncLinB-DmbA has the highest active site cavity volume and the biggest entrance radius on the main tunnel in comparison to descendant enzymes. Ancestral sequence reconstruction is a powerful technique to study molecular evolution and design robust proteins for enzyme technologies.
ESTHER : Mazur_2021_Int.J.Mol.Sci_22_11992
PubMedSearch : Mazur_2021_Int.J.Mol.Sci_22_11992
PubMedID: 34769421
Gene_locus related to this paper: 9zzzz-AncLinB

Title : Crystallization and Crystallographic Analysis of a Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant with an Eliminated Halide-Binding Site - Pudnikova_2019_Crystals_9_375
Author(s) : Prudnikova T , Kascakova B , Mesters JR , Grinkevich P , Havlickova P , Mazur A , Shaposhnikova A , Chaloupkova R , Damborsky J , Kuty M , Smatanova IK
Ref : , 9 :375 , 2019
Abstract : Haloalkane dehalogenases are a very important class of microbial enzymes for environmental detoxification of halogenated pollutants, for biocatalysis, biosensing and molecular tagging. The double mutant (Ile44Leu + Gln102His) of the haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94 (DbeADCl) was constructed to study the role of the second halide-binding site previously discovered in the wild-type structure. The variant is less active, less stable in the presence of chloride ions and exhibits significantly altered substrate specificity when compared with the DbeAwt. DbeADCl was crystallized using the sitting-drop vapour-diffusion procedure with further optimization by the random microseeding technique. The crystal structure of the DbeADCl has been determined and refined to the 1.4 A resolution. The DbeADCl crystals belong to monoclinic space group C121. The DbeADCl molecular structure was characterized and compared with five known haloalkane dehalogenases selected from the Protein Data Bank
ESTHER : Pudnikova_2019_Crystals_9_375
PubMedSearch : Pudnikova_2019_Crystals_9_375
Gene_locus related to this paper: brael-e2rv62

Title : A combination of spin diffusion methods for the determination of protein-ligand complex structural ensembles - Pilger_2015_Angew.Chem.Int.Ed.Engl_54_6511
Author(s) : Pilger J , Mazur A , Monecke P , Schreuder H , Elshorst B , Bartoschek S , Langer T , Schiffer A , Krimm I , Wegstroth M , Lee D , Hessler G , Wendt KU , Becker S , Griesinger C
Ref : Angew Chem Int Ed Engl , 54 :6511 , 2015
Abstract : Structure-based drug design (SBDD) is a powerful and widely used approach to optimize affinity of drug candidates. With the recently introduced INPHARMA method, the binding mode of small molecules to their protein target can be characterized even if no spectroscopic information about the protein is known. Here, we show that the combination of the spin-diffusion-based NMR methods INPHARMA, trNOE, and STD results in an accurate scoring function for docking modes and therefore determination of protein-ligand complex structures. Applications are shown on the model system protein kinase A and the drug targets glycogen phosphorylase and soluble epoxide hydrolase (sEH). Multiplexing of several ligands improves the reliability of the scoring function further. The new score allows in the case of sEH detecting two binding modes of the ligand in its binding site, which was corroborated by X-ray analysis.
ESTHER : Pilger_2015_Angew.Chem.Int.Ed.Engl_54_6511
PubMedSearch : Pilger_2015_Angew.Chem.Int.Ed.Engl_54_6511
PubMedID: 25877959
Gene_locus related to this paper: human-EPHX2

Title : Fibroblast activation protein-alpha promotes tumor growth and invasion of breast cancer cells through non-enzymatic functions - Huang_2011_Clin.Exp.Metastasis_28_567
Author(s) : Huang Y , Simms AE , Mazur A , Wang S , Leon NR , Jones B , Aziz N , Kelly T
Ref : Clinical & Experimental Metastasisis , 28 :567 , 2011
Abstract : Fibroblast activation protein-alpha (FAP) is a cell surface, serine protease of the post-prolyl peptidase family that is expressed in human breast cancer but not in normal tissues. Previously, we showed that FAP expression increased tumor growth rates in a mouse model of human breast cancer. Here the role of the proteolytic activities of FAP in promoting tumor growth, matrix degradation and invasion was investigated. Mammary fat pads of female SCID mice were inoculated with breast cancer cells that express FAP and the mice treated with normal saline or Val-boroPro (talabostat); Glu-boroPro (PT-630); or 1-[[(3-hydroxy-1-adamantyl)amino]acetyl]-2-cyano-(S)-pyrrolidine (LAF-237) that inhibit prolyl peptidases. Other mice were injected with breast cancer cells expressing a catalytically inactive mutant of FAP and did not receive inhibitor treatment. PT-630 and LAF-237 did not slow growth of tumors produced by any of the three cell lines expressing FAP. Talabostat slightly decreased the growth rates of the FAP-expressing tumors but because PT-630 and LAF-237 did not, the growth retardation was likely not related to the inhibition of FAP or the related post-prolyl peptidase dipeptidyl peptidase IV. Breast cancer cells expressing a catalytically inactive mutant of FAP (FAP(S624A)) also produced tumors that grew rapidly. In vitro studies revealed that cells expressing wild type FAP or FAP(S624A) degrade extracellular matrix (ECM) more extensively, accumulate higher levels of matrix metalloproteinase-9 (MMP-9) in conditioned medium, are more invasive in type I collagen gels, and have altered signaling compared to control transfectants that do not express FAP and form slow growing tumors. We conclude that the proteolytic activity of FAP participates in matrix degradation, but other functions of the protein stimulate increased tumor growth.
ESTHER : Huang_2011_Clin.Exp.Metastasis_28_567
PubMedSearch : Huang_2011_Clin.Exp.Metastasis_28_567
PubMedID: 21604185

Title : Secreted lipases of Candida albicans: cloning, characterisation and expression analysis of a new gene family with at least ten members - Hube_2000_Arch.Microbiol_174_362
Author(s) : Hube B , Stehr F , Bossenz M , Mazur A , Kretschmar M , Schafer W
Ref : Arch Microbiol , 174 :362 , 2000
Abstract : Extracellular lipolytic activity enabled the human pathogen Candida albicans to grow on lipids as the sole source of carbon. Nine new members of a lipase gene family (LIP2-LIP10) with high similarities to the recently cloned lipase gene LIP1 were cloned and characterised. The ORFs of all ten lipase genes are between 1281 and 1416 bp long and encode highly similar proteins with up to 80% identical amino acid sequences. Each deduced lipase sequence has conserved lipase motifs, four conserved cysteine residues, conserved putative N-glycosylation sites and similar hydrophobicity profiles. All LIP genes, except LIP7, also encode an N-terminal signal sequence. LIP3-LIP6 were expressed in all media and at all time points of growth tested as shown by Northern blot and RT-PCR analyses. LIP1, LIP3, LIP4, LIP5, LIP6 and LIP8 were expressed in medium with Tween 40 as a sole source of carbon. However, the same genes were also expressed in media without lipids. Two other genes, LIP2 and LIP9, were only expressed in media lacking lipids. Transcripts of most lipase genes were detected during the yeast-to-hyphal transition. Furthermore, LIP5, LIP6, LIP8 and LIP9 were found to be expressed during experimental infection of mice. These data indicate lipid-independent, highly flexible in vitro and in vivo expression of a large number of LIP genes, possibly reflecting broad lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue.
ESTHER : Hube_2000_Arch.Microbiol_174_362
PubMedSearch : Hube_2000_Arch.Microbiol_174_362
PubMedID: 11131027
Gene_locus related to this paper: canal-LIP1 , canal-LIP2 , canal-LIP3 , canal-LIP4 , canal-LIP5 , canal-LIP6 , canal-LIP7 , canal-LIP8 , canal-LIP9 , canal-LIP10

Title : Mechanism of in vitro and in vivo inhibition of cholinesterase activity by diisopropyl fluorophosphate -
Author(s) : Bodansky O , Mazur A
Ref : Federation Proceedings , 5 :123 , 1946
PubMedID: 21066635

Title : An enzyme in animal tissues capable of hydrolyzing the phosphorus-fluorine bond of alkyl fluorophosphates -
Author(s) : Mazur A
Ref : Journal of Biological Chemistry , 164 :271 , 1946