The Experts below are selected from a list of 258 Experts worldwide ranked by ideXlab platform
Markus Perbandt - One of the best experts on this subject based on the ideXlab platform.
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Structure of ThiM from Vitamin B1 biosynthetic pathway of Staphylococcus aureus - Insights into a novel pro-drug approach addressing MRSA infections.
Scientific reports, 2016Co-Authors: Julia Drebes, Madeleine Kunz, Björn Windshügel, Alexey Kikhney, Ingrid Müller, Raphael J. Eberle, Dominik Oberthür, Huaixing Cang, Dmitri I. Svergun, Markus PerbandtAbstract:Infections caused by the methicillin-resistant Staphylococcus aureus (MRSA) are today known to be a substantial threat for global health. Emerging multi-drug resistant bacteria have created a substantial need to identify and discover new drug targets and to develop novel strategies to treat bacterial infections. A promising and so far untapped antibiotic target is the biosynthesis of vitamin B1 (thiamin). Thiamin in its activated form, thiamin pyrophosphate, is an essential co-factor for all organisms. Therefore, thiamin analogous compounds, when introduced into the vitamin B1 biosynthetic pathway and further converted into non-functional co-factors by the bacterium can function as pro-drugs which thus block various co-factor dependent pathways. We characterized one of the key enzymes within the S. aureus vitamin B1 biosynthetic pathway, 5-(hydroxyethyl)-4-Methylthiazole kinase (SaThiM; EC 2.7.1.50), a potential target for pro-drug compounds and analyzed the native structure of SaThiM and complexes with the natural substrate 5-(hydroxyethyl)-4-Methylthiazole (THZ) and two selected substrate analogues.
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Purification, crystallization and preliminary X-ray diffraction analysis of ThiM from Staphylococcus aureus.
Acta Crystallographica Section F-structural Biology and Crystallization Communications, 2011Co-Authors: Julia Drebes, Markus Perbandt, Carsten Wrenger, Christian BetzelAbstract:ThiM [5-(hydroxyethyl)-4-Methylthiazole kinase; EC 2.7.1.50] from Staphylococcus aureus is an essential enzyme of thiamine or vitamin B1 metabolism and has been crystallized by the vapour-diffusion method. The crystals belonged to the primitive space group P1, with unit-cell parameters a = 62.06, b = 62.40, c = 107.82 A, α = 92.25, β = 91.37, γ = 101.48° and six protomers in the unit cell, corresponding to a packing parameter VM of 2.3 A3 Da−1. Diffraction data were collected to 2.1 A resolution using synchrotron radiation. The phase problem was solved by molecular replacement.
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Purification, crystallization and preliminary X-ray diffraction analysis of the thiaminase type II from Staphylococcus aureus.
Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2010Co-Authors: Afshan Begum, Julia Drebes, Markus Perbandt, Carsten Wrenger, Christian BetzelAbstract:Thiaminase type II (TenA) catalyzes the deamination of aminopyrimidines, including the cleavage of thiamine to 4-amino-5-hydroxymethyl-2-methylpyrimidine and 5-(2-hydroxyethyl)-4-Methylthiazole in the metabolism of thiamine (vitamin B1), in Staphylococcus aureus (Sa). SaTenA was crystallized by the vapour-diffusion method and the resulting crystal diffracted to 2.6 Å resolution usng synchrotron radiation. The crystal is orthorhombic, belonging to space group P2(1)2(1)2(1) with unit-cell parameters a=103.5, b=104.1, c=109.6 Å. With four molecules in the asymmetric unit, the Matthews coefficient is 2.85 Å3 Da(-1). Initial attempts to solve the structure by molecular-replacement techniques were successful
O V Gorokhova - One of the best experts on this subject based on the ideXlab platform.
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4 hydroxy 2 quinolones 90 synthesis and antitubercular activity of 4 methyl 2 thiazolylamides of halo substituted 4 hydroxy 2 oxo 1 2 dihydro 3 quinolinecarboxylic acids
Chemistry of Heterocyclic Compounds, 2006Co-Authors: I V Ukrainets, L V Sidorenko, Lidiya A Petrushova, O V GorokhovaAbstract:Several variants were studied for the synthesis of esters of halogen derivatives of 4-hydroxy-2-oxo-1,2-dihydro-3-quinolinecarboxylic acids, whose reaction with 2-amino-4-Methylthiazole gives the corresponding hetarylamides. Results are given for a study of the antitubercular activity of these products.
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4-HYDROXY-2-QUINOLONES. 90.* SYNTHESIS AND ANTITUBERCULAR ACTIVITY OF 4-METHYL- 2-THIAZOLYLAMIDES OF HALO-SUBSTITUTED 4-HYDROXY-2-OXO-1,2-DIHYDRO- 3-QUINOLINECARBOXYLIC ACIDS
Chemistry of Heterocyclic Compounds, 2006Co-Authors: I V Ukrainets, L V Sidorenko, Lidiya A Petrushova, O V GorokhovaAbstract:Several variants were studied for the synthesis of esters of halogen derivatives of 4-hydroxy-2-oxo-1,2-dihydro-3-quinolinecarboxylic acids, whose reaction with 2-amino-4-Methylthiazole gives the corresponding hetarylamides. Results are given for a study of the antitubercular activity of these products.
Julia Drebes - One of the best experts on this subject based on the ideXlab platform.
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Structure of ThiM from Vitamin B1 biosynthetic pathway of Staphylococcus aureus - Insights into a novel pro-drug approach addressing MRSA infections.
Scientific reports, 2016Co-Authors: Julia Drebes, Madeleine Kunz, Björn Windshügel, Alexey Kikhney, Ingrid Müller, Raphael J. Eberle, Dominik Oberthür, Huaixing Cang, Dmitri I. Svergun, Markus PerbandtAbstract:Infections caused by the methicillin-resistant Staphylococcus aureus (MRSA) are today known to be a substantial threat for global health. Emerging multi-drug resistant bacteria have created a substantial need to identify and discover new drug targets and to develop novel strategies to treat bacterial infections. A promising and so far untapped antibiotic target is the biosynthesis of vitamin B1 (thiamin). Thiamin in its activated form, thiamin pyrophosphate, is an essential co-factor for all organisms. Therefore, thiamin analogous compounds, when introduced into the vitamin B1 biosynthetic pathway and further converted into non-functional co-factors by the bacterium can function as pro-drugs which thus block various co-factor dependent pathways. We characterized one of the key enzymes within the S. aureus vitamin B1 biosynthetic pathway, 5-(hydroxyethyl)-4-Methylthiazole kinase (SaThiM; EC 2.7.1.50), a potential target for pro-drug compounds and analyzed the native structure of SaThiM and complexes with the natural substrate 5-(hydroxyethyl)-4-Methylthiazole (THZ) and two selected substrate analogues.
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Purification, crystallization and preliminary X-ray diffraction analysis of ThiM from Staphylococcus aureus.
Acta Crystallographica Section F-structural Biology and Crystallization Communications, 2011Co-Authors: Julia Drebes, Markus Perbandt, Carsten Wrenger, Christian BetzelAbstract:ThiM [5-(hydroxyethyl)-4-Methylthiazole kinase; EC 2.7.1.50] from Staphylococcus aureus is an essential enzyme of thiamine or vitamin B1 metabolism and has been crystallized by the vapour-diffusion method. The crystals belonged to the primitive space group P1, with unit-cell parameters a = 62.06, b = 62.40, c = 107.82 A, α = 92.25, β = 91.37, γ = 101.48° and six protomers in the unit cell, corresponding to a packing parameter VM of 2.3 A3 Da−1. Diffraction data were collected to 2.1 A resolution using synchrotron radiation. The phase problem was solved by molecular replacement.
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Purification, crystallization and preliminary X-ray diffraction analysis of the thiaminase type II from Staphylococcus aureus.
Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2010Co-Authors: Afshan Begum, Julia Drebes, Markus Perbandt, Carsten Wrenger, Christian BetzelAbstract:Thiaminase type II (TenA) catalyzes the deamination of aminopyrimidines, including the cleavage of thiamine to 4-amino-5-hydroxymethyl-2-methylpyrimidine and 5-(2-hydroxyethyl)-4-Methylthiazole in the metabolism of thiamine (vitamin B1), in Staphylococcus aureus (Sa). SaTenA was crystallized by the vapour-diffusion method and the resulting crystal diffracted to 2.6 Å resolution usng synchrotron radiation. The crystal is orthorhombic, belonging to space group P2(1)2(1)2(1) with unit-cell parameters a=103.5, b=104.1, c=109.6 Å. With four molecules in the asymmetric unit, the Matthews coefficient is 2.85 Å3 Da(-1). Initial attempts to solve the structure by molecular-replacement techniques were successful
I V Ukrainets - One of the best experts on this subject based on the ideXlab platform.
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4 hydroxy 2 quinolones 90 synthesis and antitubercular activity of 4 methyl 2 thiazolylamides of halo substituted 4 hydroxy 2 oxo 1 2 dihydro 3 quinolinecarboxylic acids
Chemistry of Heterocyclic Compounds, 2006Co-Authors: I V Ukrainets, L V Sidorenko, Lidiya A Petrushova, O V GorokhovaAbstract:Several variants were studied for the synthesis of esters of halogen derivatives of 4-hydroxy-2-oxo-1,2-dihydro-3-quinolinecarboxylic acids, whose reaction with 2-amino-4-Methylthiazole gives the corresponding hetarylamides. Results are given for a study of the antitubercular activity of these products.
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4-HYDROXY-2-QUINOLONES. 90.* SYNTHESIS AND ANTITUBERCULAR ACTIVITY OF 4-METHYL- 2-THIAZOLYLAMIDES OF HALO-SUBSTITUTED 4-HYDROXY-2-OXO-1,2-DIHYDRO- 3-QUINOLINECARBOXYLIC ACIDS
Chemistry of Heterocyclic Compounds, 2006Co-Authors: I V Ukrainets, L V Sidorenko, Lidiya A Petrushova, O V GorokhovaAbstract:Several variants were studied for the synthesis of esters of halogen derivatives of 4-hydroxy-2-oxo-1,2-dihydro-3-quinolinecarboxylic acids, whose reaction with 2-amino-4-Methylthiazole gives the corresponding hetarylamides. Results are given for a study of the antitubercular activity of these products.
Alexey Kikhney - One of the best experts on this subject based on the ideXlab platform.
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Structure of ThiM from Vitamin B1 biosynthetic pathway of Staphylococcus aureus - Insights into a novel pro-drug approach addressing MRSA infections.
Scientific reports, 2016Co-Authors: Julia Drebes, Madeleine Kunz, Björn Windshügel, Alexey Kikhney, Ingrid Müller, Raphael J. Eberle, Dominik Oberthür, Huaixing Cang, Dmitri I. Svergun, Markus PerbandtAbstract:Infections caused by the methicillin-resistant Staphylococcus aureus (MRSA) are today known to be a substantial threat for global health. Emerging multi-drug resistant bacteria have created a substantial need to identify and discover new drug targets and to develop novel strategies to treat bacterial infections. A promising and so far untapped antibiotic target is the biosynthesis of vitamin B1 (thiamin). Thiamin in its activated form, thiamin pyrophosphate, is an essential co-factor for all organisms. Therefore, thiamin analogous compounds, when introduced into the vitamin B1 biosynthetic pathway and further converted into non-functional co-factors by the bacterium can function as pro-drugs which thus block various co-factor dependent pathways. We characterized one of the key enzymes within the S. aureus vitamin B1 biosynthetic pathway, 5-(hydroxyethyl)-4-Methylthiazole kinase (SaThiM; EC 2.7.1.50), a potential target for pro-drug compounds and analyzed the native structure of SaThiM and complexes with the natural substrate 5-(hydroxyethyl)-4-Methylthiazole (THZ) and two selected substrate analogues.
