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Ditlev E. Brodersen - One of the best experts on this subject based on the ideXlab platform.
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Structural insights into the bacterial carbon–phosphorus lyase machinery
Nature, 2015Co-Authors: Paulina Seweryn, Lan Bich Van, Morten Kjeldgaard, Christopher J. Russo, Lori A. Passmore, Bjarne Hove-jensen, Bjarne Jochimsen, Ditlev E. BrodersenAbstract:The crystal structure of the 240-kilodalton C–P lyase core complex from the bacterium E. coli offers insights into the relatively unknown mechanisms of the enzymatic machinery that allows some microbes to extract phosphate from Phosphonate compounds. Phosphorus is required for all life and microorganisms can extract it from their environment through several metabolic pathways. When phosphate is in limited supply, some bacteria are able to use Phosphonate compounds, which require specialized enzymatic machinery to break the stable carbon–phosphorus (C–P) bond. Despite its importance, the details of how this machinery catabolizes Phosphonates remain unknown. Here we determine the crystal structure of the 240-kilodalton Escherichia coli C–P lyase core complex (PhnG–PhnH–PhnI–PhnJ; PhnGHIJ), and show that it is a two-fold symmetric hetero-octamer comprising an intertwined network of subunits with unexpected self-homologies. It contains two potential active sites that probably couple Phosphonate compounds to ATP and subsequently hydrolyse the C–P bond. We map the binding site of PhnK on the complex using electron microscopy, and show that it binds to a conserved insertion domain of PhnJ. Our results provide a structural basis for understanding microbial Phosphonate breakdown. When phosphates are in short supply, certain bacteria are able to utilize Organic Phosphonate compounds thanks to specialized enzymatic machinery that breaks the stable carbon–phosphorus bond. The mechanism involved is not clear. Ditlev Brodersen and colleagues have determined the crystal structure of the 240-kilodalton C–P lyase complex from Escherichia coli . The structure contains two potential active sites that may couple Organic Phosphonate compounds to ATP and subsequently hydrolyse the C–P bond.
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Crystal Structure of the Carbon-Phosphorus Lyase Complex from Escherichia coli
Acta Crystallographica Section A Foundations and Advances, 2014Co-Authors: Paulina Seweryn, Morten Kjeldgaard, Bjarne Hove-jensen, Bjarne Jochimsen, Lan Van, Ditlev E. BrodersenAbstract:Phosphorus is an essential element for all living cells and is usually taken up in the form of phosphate. A number of microorganisms, however, are capable of extracting phosphorous from Organic Phosphonate compounds, which are characterized by a stable carbon-phosphorus (C-P) bond (1). The metabolic pathway responsible for Phosphonate degradation is still poorly understood, but the process is known to involve two reactions before the actual C-P bond cleavage, which has been proposed to take place via a radical mechanism. A key component in the process is C-P lyase, an enzyme encoded by phnJ within the phn operon (2). To get a better insight into the mechanism of this complex degradation pathway, we have determined the crystal structure of the core of a multi-subunit enzymatic complex including the C-P lyase component with a total molecular mass of 220 kDa (3). The structure reveals the overall architecture of the C-P lyase and has important implications for our understanding of enzyme mechanism and catalysis.
Guosheng Yang - One of the best experts on this subject based on the ideXlab platform.
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Study of Elution Order in Chiral Separation of OrganoPhosphonate Esters Using Tris-(3,5-dimethylphenyl Carbamate) Cellulose Chiral Stationary Phase by HPLC
Journal of Liquid Chromatography & Related Technologies, 2009Co-Authors: Bing Liu, Guosheng Yang, Hassan Y. Aboul-eneinAbstract:It is known that the separation of several Organic Phosphonate esters using a tris(3,5-dimethylphenyl carbamate) cellulose (Chiralcel OD) column are better than the separation obtained using the Pirkle type chiral stationary phase (CSP), namely the N-(3,5-dinitrobenzoyl) leucine column. However, the elution order of the Organic Phosphonate esters enantiomers separated on tris(3,5-dimethylphenyl carbamate) cellulose chiral stationary phase is not known. The tandem use of these two CSPs together showed that the R-enantiomer had shorter retention time than S-enantiomer when tris(3,5-dimethylphenyl carbamate) cellulose chiral stationary phase was used.
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Chiral Separation of Organic Phosphonate Compounds on Polysaccharide-Based Chiral Stationary Phases
Chromatographia, 2004Co-Authors: Guosheng Yang, C. Y. Zhan, P. Parrilla Vázquez, A. Garrido Frenich, J. L. Martínez Vidal, Hassan Y. Aboul-eneinAbstract:Four polysaccharide-based chiral stationary phases have been used to separate the enantiomers of fourteen O,O-dialkyl-1-benzyloxycarbonyl-aminoarylmethyl Phosphonates. These polysaccharide-based chiral stationary phases are Chiralpak AD, Chiralpak AS, Chiralcel OG and Chiralcel OJ. The data obtained indicate that the chiral separation ability for these organoPhosphonate compounds are in the order Chiralpak AD > Chiralcel OG > Chiralcel OJ > Chiralpak AS. With Chiralpak AD, all of the studied compounds could be easily baseline separated. Those two polysaccharides possess different chiral discrimination mechanism due to of the difference of the conformational structures of amylose and cellulose. The chiral discrimination of derivatized amylose chiral stationary phases were based on the stereogenic fit of the analytes in the helical structures of amylose and the transient diastereomeric complex formation between the analyte and the amylose CSP through π–π interaction H-bond interactions and induced dipole interactions exerted by the substituents on the analyte molecules. The chiral discrimination, in case of derivatized cellulose chiral stationary phase is based on the stereogenic fit of the analytes in the grooves of cellulose followed by interactions mentioned above between the analytes and the cellulose CSP.
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Enantioseparation of 15 Organic Phosphonate esters on the cellulose tris(3,5-dimethylphenyl carbamate) chiral stationary phase by HPLC.
Talanta, 2003Co-Authors: Guosheng Yang, Xinqiang Wang, Shi-ling Yuan, Lan Zhou, Chengpu LiuAbstract:A series of 15 Organic Phosphonate esters enatiomers containing a carbon atom as a chiral center have been separated on the cellulose tris(3,5-dimethylphenyl carbamate) chiral stationary phase (CSP) in the normal phase by high performance liquid chromatography (HPLC). Both the capacity factor (k) and separation factor (α) of all solutes are presented. The influence of the substitutional group on the benzene ring attached to the chiral carbon atom and the steric hindrance of alkoxyl of the Phosphonate ester on the chiral separation are discussed. Based on α and different structure parameters, good agreement between the predicted values and the experimental ones is obtained. The most characteristic parameter influencing the chromatographic separation is chosen from many structure parameters by linear regression method of QSAR software. The probable mechanism of the chiral recognition is proposed.
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Chiral Separation of Organic Phosphonate Compounds on Cellulose CSP (Chiral Stationary Phase) under Reversed Phase Mode
Analytical Sciences, 2003Co-Authors: Guosheng Yang, A. Garrido Frenich, J. L. Martínez Vidal, Piedad Parrilla Vázquez, Hassan Y. Aboul-eneinAbstract:The enantiomers of fourteen O,O-dialkyl-2-benzyloxycarbonyl-aminoarylmethyl-Phosphonates are directly separated on the tris(3,5-dimethylphenylcarbamate) cellulose column (Chiralcel OD-R) under reversed phase mode. The results of the chiral separation are different from the results obtained in the normal phase mode. The mobile phase plays an essential role in chiral discrimination when using Chiralcel OD-R. The influences of the mobile phase composition on the retention and the enantioselectivity are investigated. The influences on chiral separation of the length and steric hindrance of alkoxy groups of the Phosphonate ester and of the nature of the substituent on the benzene ring that is attached to the chiral carbon atom are also discussed.
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Effect of the Structure of Organic Phosphonate Compounds on Chiral Separations on Derivatized Cellulose Chiral Stationary Phase
Chromatographia, 2002Co-Authors: Guosheng Yang, Lan Zhou, P. Parrilla Vázquez, Du Wei, A. Garrido FrenichAbstract:The enantiomers of eightO,O-dialkyl-2-benzyloxycarbonylaminoarylmethyl Phosphonates have been directly separated on a tris(3,5-dimethylphenylcarbamate) cellulose column. The results are very different from those obtained by separation on anN-(3,5-dinitrobenzoyl)leucine (DNBleu) column. The effect of mobile phase composition and column temperature on retention and enantioselectivity were investigated. The effect on chiral separation of the length of, and steric hindrance by, alkoxyl groups of the Phosphonate ester and of the nature of the substitutentsp-Cl andp-H on the benzene ring attached to the chiral carbon atom are also discussed.
Hassan Y. Aboul-enein - One of the best experts on this subject based on the ideXlab platform.
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Study of Elution Order in Chiral Separation of OrganoPhosphonate Esters Using Tris-(3,5-dimethylphenyl Carbamate) Cellulose Chiral Stationary Phase by HPLC
Journal of Liquid Chromatography & Related Technologies, 2009Co-Authors: Bing Liu, Guosheng Yang, Hassan Y. Aboul-eneinAbstract:It is known that the separation of several Organic Phosphonate esters using a tris(3,5-dimethylphenyl carbamate) cellulose (Chiralcel OD) column are better than the separation obtained using the Pirkle type chiral stationary phase (CSP), namely the N-(3,5-dinitrobenzoyl) leucine column. However, the elution order of the Organic Phosphonate esters enantiomers separated on tris(3,5-dimethylphenyl carbamate) cellulose chiral stationary phase is not known. The tandem use of these two CSPs together showed that the R-enantiomer had shorter retention time than S-enantiomer when tris(3,5-dimethylphenyl carbamate) cellulose chiral stationary phase was used.
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Chiral Separation of Organic Phosphonate Compounds on Polysaccharide-Based Chiral Stationary Phases
Chromatographia, 2004Co-Authors: Guosheng Yang, C. Y. Zhan, P. Parrilla Vázquez, A. Garrido Frenich, J. L. Martínez Vidal, Hassan Y. Aboul-eneinAbstract:Four polysaccharide-based chiral stationary phases have been used to separate the enantiomers of fourteen O,O-dialkyl-1-benzyloxycarbonyl-aminoarylmethyl Phosphonates. These polysaccharide-based chiral stationary phases are Chiralpak AD, Chiralpak AS, Chiralcel OG and Chiralcel OJ. The data obtained indicate that the chiral separation ability for these organoPhosphonate compounds are in the order Chiralpak AD > Chiralcel OG > Chiralcel OJ > Chiralpak AS. With Chiralpak AD, all of the studied compounds could be easily baseline separated. Those two polysaccharides possess different chiral discrimination mechanism due to of the difference of the conformational structures of amylose and cellulose. The chiral discrimination of derivatized amylose chiral stationary phases were based on the stereogenic fit of the analytes in the helical structures of amylose and the transient diastereomeric complex formation between the analyte and the amylose CSP through π–π interaction H-bond interactions and induced dipole interactions exerted by the substituents on the analyte molecules. The chiral discrimination, in case of derivatized cellulose chiral stationary phase is based on the stereogenic fit of the analytes in the grooves of cellulose followed by interactions mentioned above between the analytes and the cellulose CSP.
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Chiral Separation of Organic Phosphonate Compounds on Cellulose CSP (Chiral Stationary Phase) under Reversed Phase Mode
Analytical Sciences, 2003Co-Authors: Guosheng Yang, A. Garrido Frenich, J. L. Martínez Vidal, Piedad Parrilla Vázquez, Hassan Y. Aboul-eneinAbstract:The enantiomers of fourteen O,O-dialkyl-2-benzyloxycarbonyl-aminoarylmethyl-Phosphonates are directly separated on the tris(3,5-dimethylphenylcarbamate) cellulose column (Chiralcel OD-R) under reversed phase mode. The results of the chiral separation are different from the results obtained in the normal phase mode. The mobile phase plays an essential role in chiral discrimination when using Chiralcel OD-R. The influences of the mobile phase composition on the retention and the enantioselectivity are investigated. The influences on chiral separation of the length and steric hindrance of alkoxy groups of the Phosphonate ester and of the nature of the substituent on the benzene ring that is attached to the chiral carbon atom are also discussed.
Paulina Seweryn - One of the best experts on this subject based on the ideXlab platform.
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Structural insights into the bacterial carbon–phosphorus lyase machinery
Nature, 2015Co-Authors: Paulina Seweryn, Lan Bich Van, Morten Kjeldgaard, Christopher J. Russo, Lori A. Passmore, Bjarne Hove-jensen, Bjarne Jochimsen, Ditlev E. BrodersenAbstract:The crystal structure of the 240-kilodalton C–P lyase core complex from the bacterium E. coli offers insights into the relatively unknown mechanisms of the enzymatic machinery that allows some microbes to extract phosphate from Phosphonate compounds. Phosphorus is required for all life and microorganisms can extract it from their environment through several metabolic pathways. When phosphate is in limited supply, some bacteria are able to use Phosphonate compounds, which require specialized enzymatic machinery to break the stable carbon–phosphorus (C–P) bond. Despite its importance, the details of how this machinery catabolizes Phosphonates remain unknown. Here we determine the crystal structure of the 240-kilodalton Escherichia coli C–P lyase core complex (PhnG–PhnH–PhnI–PhnJ; PhnGHIJ), and show that it is a two-fold symmetric hetero-octamer comprising an intertwined network of subunits with unexpected self-homologies. It contains two potential active sites that probably couple Phosphonate compounds to ATP and subsequently hydrolyse the C–P bond. We map the binding site of PhnK on the complex using electron microscopy, and show that it binds to a conserved insertion domain of PhnJ. Our results provide a structural basis for understanding microbial Phosphonate breakdown. When phosphates are in short supply, certain bacteria are able to utilize Organic Phosphonate compounds thanks to specialized enzymatic machinery that breaks the stable carbon–phosphorus bond. The mechanism involved is not clear. Ditlev Brodersen and colleagues have determined the crystal structure of the 240-kilodalton C–P lyase complex from Escherichia coli . The structure contains two potential active sites that may couple Organic Phosphonate compounds to ATP and subsequently hydrolyse the C–P bond.
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Crystal Structure of the Carbon-Phosphorus Lyase Complex from Escherichia coli
Acta Crystallographica Section A Foundations and Advances, 2014Co-Authors: Paulina Seweryn, Morten Kjeldgaard, Bjarne Hove-jensen, Bjarne Jochimsen, Lan Van, Ditlev E. BrodersenAbstract:Phosphorus is an essential element for all living cells and is usually taken up in the form of phosphate. A number of microorganisms, however, are capable of extracting phosphorous from Organic Phosphonate compounds, which are characterized by a stable carbon-phosphorus (C-P) bond (1). The metabolic pathway responsible for Phosphonate degradation is still poorly understood, but the process is known to involve two reactions before the actual C-P bond cleavage, which has been proposed to take place via a radical mechanism. A key component in the process is C-P lyase, an enzyme encoded by phnJ within the phn operon (2). To get a better insight into the mechanism of this complex degradation pathway, we have determined the crystal structure of the core of a multi-subunit enzymatic complex including the C-P lyase component with a total molecular mass of 220 kDa (3). The structure reveals the overall architecture of the C-P lyase and has important implications for our understanding of enzyme mechanism and catalysis.
Bjarne Hove-jensen - One of the best experts on this subject based on the ideXlab platform.
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Structural insights into the bacterial carbon–phosphorus lyase machinery
Nature, 2015Co-Authors: Paulina Seweryn, Lan Bich Van, Morten Kjeldgaard, Christopher J. Russo, Lori A. Passmore, Bjarne Hove-jensen, Bjarne Jochimsen, Ditlev E. BrodersenAbstract:The crystal structure of the 240-kilodalton C–P lyase core complex from the bacterium E. coli offers insights into the relatively unknown mechanisms of the enzymatic machinery that allows some microbes to extract phosphate from Phosphonate compounds. Phosphorus is required for all life and microorganisms can extract it from their environment through several metabolic pathways. When phosphate is in limited supply, some bacteria are able to use Phosphonate compounds, which require specialized enzymatic machinery to break the stable carbon–phosphorus (C–P) bond. Despite its importance, the details of how this machinery catabolizes Phosphonates remain unknown. Here we determine the crystal structure of the 240-kilodalton Escherichia coli C–P lyase core complex (PhnG–PhnH–PhnI–PhnJ; PhnGHIJ), and show that it is a two-fold symmetric hetero-octamer comprising an intertwined network of subunits with unexpected self-homologies. It contains two potential active sites that probably couple Phosphonate compounds to ATP and subsequently hydrolyse the C–P bond. We map the binding site of PhnK on the complex using electron microscopy, and show that it binds to a conserved insertion domain of PhnJ. Our results provide a structural basis for understanding microbial Phosphonate breakdown. When phosphates are in short supply, certain bacteria are able to utilize Organic Phosphonate compounds thanks to specialized enzymatic machinery that breaks the stable carbon–phosphorus bond. The mechanism involved is not clear. Ditlev Brodersen and colleagues have determined the crystal structure of the 240-kilodalton C–P lyase complex from Escherichia coli . The structure contains two potential active sites that may couple Organic Phosphonate compounds to ATP and subsequently hydrolyse the C–P bond.
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Crystal Structure of the Carbon-Phosphorus Lyase Complex from Escherichia coli
Acta Crystallographica Section A Foundations and Advances, 2014Co-Authors: Paulina Seweryn, Morten Kjeldgaard, Bjarne Hove-jensen, Bjarne Jochimsen, Lan Van, Ditlev E. BrodersenAbstract:Phosphorus is an essential element for all living cells and is usually taken up in the form of phosphate. A number of microorganisms, however, are capable of extracting phosphorous from Organic Phosphonate compounds, which are characterized by a stable carbon-phosphorus (C-P) bond (1). The metabolic pathway responsible for Phosphonate degradation is still poorly understood, but the process is known to involve two reactions before the actual C-P bond cleavage, which has been proposed to take place via a radical mechanism. A key component in the process is C-P lyase, an enzyme encoded by phnJ within the phn operon (2). To get a better insight into the mechanism of this complex degradation pathway, we have determined the crystal structure of the core of a multi-subunit enzymatic complex including the C-P lyase component with a total molecular mass of 220 kDa (3). The structure reveals the overall architecture of the C-P lyase and has important implications for our understanding of enzyme mechanism and catalysis.