Michael Danson - Academia.edu (original) (raw)

Uploads

Papers by Michael Danson

Research paper thumbnail of A comparison of ELISA screening methods for the production of monoclonal antibodies against soluble protein antigens

Journal of Immunological Methods, Oct 1, 1986

A library of monoclonal antibodies against pig heart citrate synthase has been raised. Twelve sol... more A library of monoclonal antibodies against pig heart citrate synthase has been raised. Twelve solid-phase immunoassay systems, employing different methods of antigen immobilization, have been compared for their ability to detect the various members of this library. It was found that a sandwich immunoassay, in which the citrate synthase antigen was immobilized on the solid support via a polyclonal antibody preparation, was the only system capable of detecting all the monoclonal antibodies tested. It is suggested that such a sandwich assay should be used in preference to direct assays for the initial screening of monoclonal antibodies.

Research paper thumbnail of A Thermostable Aldolase for the Synthesis of 3-Deoxy-2-ulosonic Acids

Advanced Synthesis & Catalysis, Apr 2, 2007

Research paper thumbnail of Sulfolobus solfataricus Glucose Dehydrogenase 1 in complex with NADP

Research paper thumbnail of The Effect of Cysteine-43 Mutation on Thermostability and Kinetic Properties of Citrate Synthase fromThermoplasma acidophilum

Biochemical and Biophysical Research Communications, Jul 1, 1996

Research paper thumbnail of Engineering stereocontrol into aldolase catalyzed reactions

Abstracts of Papers of The American Chemical Society, 2009

Research paper thumbnail of The 2-oxoacid dehydrogenase multienzyme complex of Haloferax volcanii

Extremophiles, Jun 15, 2007

Research paper thumbnail of Cloning, sequencing, and expression of Trypanosoma brucei dihydrolipoamide dehydrogenase

European journal of biochemistry, Mar 1, 1993

Research paper thumbnail of 2-Oxoacid dehydrogenase multienzyme complexes in the halophilic Archaea? Gene sequences and protein structural predictions The GenBank accession number for the sequence reported in this paper is AF068743

Microbiology, May 1, 2000

Research paper thumbnail of Structurally Informed Site-Directed Mutagenesis of a Stereochemically Promiscuous Aldolase To Afford Stereochemically Complementary Biocatalysts

Journal of the American Chemical Society, Aug 4, 2010

2-Keto-3-deoxygluconate aldolase from the hyperthermophile Sulfolobus solfataricus is a highly th... more 2-Keto-3-deoxygluconate aldolase from the hyperthermophile Sulfolobus solfataricus is a highly thermostable type I aldolase that can catalyze carbon-carbon bond formation using nonphosphorylated substrates. However, it exhibits poor diastereocontrol in many of its aldol reactions, including the reaction of its natural substrates, pyruvate and D-glyceraldehyde, which afford a 55:45 mixture of D-2-keto-3-deoxygluconate (D-KDGlu) and D-2-keto-3-deoxy-galactonate (D-KDGal). We have employed detailed X-ray crystallographic structural information of this aldolase bound to these diastereoisomeric aldol products to selectively target specific amino acids for mutation for the rapid creation of stereochemically complementary mutants that catalyze either (Re)- or (Si)-facial selective aldol reactions to afford either D-KDGlu or D-KDGal with good levels of diastereocontrol.

Research paper thumbnail of Solution NMR structure of E2 lipoyl domain from Thermoplasma acidophilum

Research paper thumbnail of Sulfolobus solfataricus 2-keto-3-deoxygluconate (KDG) aldolase complex with D-KDGal, D-Glyceraldehyde and pyruvate

Research paper thumbnail of 531 Polymorphisms and disease: hotspots of inactivation in methyltransferases 539 Induced fit, conformational selection and independent dynamic segments: an extended view of binding events

Research paper thumbnail of Kinetics and Mechanism of the Citrate Synthase from the Thermophilic Archaeon <i>Thermoplasma acidophilum</i>

Biochemistry, Feb 12, 2000

Research paper thumbnail of Functional groups in the activity and regulation of <i>Escherichia coli</i> citrate synthase

Biochemical Journal, Nov 1, 1973

Research paper thumbnail of The thermal behaviour of enzyme activity: implications for biotechnology

Trends in Biotechnology, Jul 1, 2006

Research paper thumbnail of Sequencing and Expression of the Gene Encoding a Cold-Active Citrate Synthase from an Antarctic Bacterium, Strain DS2-3R

European journal of biochemistry, Aug 15, 1997

Research paper thumbnail of In vitro hydrogen production by glucose dehydrogenase and hydrogenase

Nature Biotechnology, Jul 1, 1996

A new in vitro enzymatic pathway for the generation of molecular hydrogen from glucose has been d... more A new in vitro enzymatic pathway for the generation of molecular hydrogen from glucose has been demonstrated. The reaction is based on the oxidation of glucose by Thermoplasma acidophilum glucose dehydrogenase with the concomitant oxidation of NADPH by Pyrococcus furiosus hydrogenase. Stoichiometric yields of hydrogen were produced from glucose with the continuous recycling of cofactor. This simple system may provide a method for the biological production of hydrogen from renewable sources. In addition, the other product of this reaction, gluconic acid, is a high-value chemical commodity.

Research paper thumbnail of Functional groups in the catalysis and regulation of Escherichia coli citrate synthase

Biochemical journal. Cellular aspects, Nov 1, 1972

Research paper thumbnail of Crystal structure of an Acetylating Aldehyde Dehydrogenase from Geobacillus thermoglucosidasius

Research paper thumbnail of Structure of Bacillus subtilis citrate synthase

Research paper thumbnail of A comparison of ELISA screening methods for the production of monoclonal antibodies against soluble protein antigens

Journal of Immunological Methods, Oct 1, 1986

A library of monoclonal antibodies against pig heart citrate synthase has been raised. Twelve sol... more A library of monoclonal antibodies against pig heart citrate synthase has been raised. Twelve solid-phase immunoassay systems, employing different methods of antigen immobilization, have been compared for their ability to detect the various members of this library. It was found that a sandwich immunoassay, in which the citrate synthase antigen was immobilized on the solid support via a polyclonal antibody preparation, was the only system capable of detecting all the monoclonal antibodies tested. It is suggested that such a sandwich assay should be used in preference to direct assays for the initial screening of monoclonal antibodies.

Research paper thumbnail of A Thermostable Aldolase for the Synthesis of 3-Deoxy-2-ulosonic Acids

Advanced Synthesis & Catalysis, Apr 2, 2007

Research paper thumbnail of Sulfolobus solfataricus Glucose Dehydrogenase 1 in complex with NADP

Research paper thumbnail of The Effect of Cysteine-43 Mutation on Thermostability and Kinetic Properties of Citrate Synthase fromThermoplasma acidophilum

Biochemical and Biophysical Research Communications, Jul 1, 1996

Research paper thumbnail of Engineering stereocontrol into aldolase catalyzed reactions

Abstracts of Papers of The American Chemical Society, 2009

Research paper thumbnail of The 2-oxoacid dehydrogenase multienzyme complex of Haloferax volcanii

Extremophiles, Jun 15, 2007

Research paper thumbnail of Cloning, sequencing, and expression of Trypanosoma brucei dihydrolipoamide dehydrogenase

European journal of biochemistry, Mar 1, 1993

Research paper thumbnail of 2-Oxoacid dehydrogenase multienzyme complexes in the halophilic Archaea? Gene sequences and protein structural predictions The GenBank accession number for the sequence reported in this paper is AF068743

Microbiology, May 1, 2000

Research paper thumbnail of Structurally Informed Site-Directed Mutagenesis of a Stereochemically Promiscuous Aldolase To Afford Stereochemically Complementary Biocatalysts

Journal of the American Chemical Society, Aug 4, 2010

2-Keto-3-deoxygluconate aldolase from the hyperthermophile Sulfolobus solfataricus is a highly th... more 2-Keto-3-deoxygluconate aldolase from the hyperthermophile Sulfolobus solfataricus is a highly thermostable type I aldolase that can catalyze carbon-carbon bond formation using nonphosphorylated substrates. However, it exhibits poor diastereocontrol in many of its aldol reactions, including the reaction of its natural substrates, pyruvate and D-glyceraldehyde, which afford a 55:45 mixture of D-2-keto-3-deoxygluconate (D-KDGlu) and D-2-keto-3-deoxy-galactonate (D-KDGal). We have employed detailed X-ray crystallographic structural information of this aldolase bound to these diastereoisomeric aldol products to selectively target specific amino acids for mutation for the rapid creation of stereochemically complementary mutants that catalyze either (Re)- or (Si)-facial selective aldol reactions to afford either D-KDGlu or D-KDGal with good levels of diastereocontrol.

Research paper thumbnail of Solution NMR structure of E2 lipoyl domain from Thermoplasma acidophilum

Research paper thumbnail of Sulfolobus solfataricus 2-keto-3-deoxygluconate (KDG) aldolase complex with D-KDGal, D-Glyceraldehyde and pyruvate

Research paper thumbnail of 531 Polymorphisms and disease: hotspots of inactivation in methyltransferases 539 Induced fit, conformational selection and independent dynamic segments: an extended view of binding events

Research paper thumbnail of Kinetics and Mechanism of the Citrate Synthase from the Thermophilic Archaeon <i>Thermoplasma acidophilum</i>

Biochemistry, Feb 12, 2000

Research paper thumbnail of Functional groups in the activity and regulation of <i>Escherichia coli</i> citrate synthase

Biochemical Journal, Nov 1, 1973

Research paper thumbnail of The thermal behaviour of enzyme activity: implications for biotechnology

Trends in Biotechnology, Jul 1, 2006

Research paper thumbnail of Sequencing and Expression of the Gene Encoding a Cold-Active Citrate Synthase from an Antarctic Bacterium, Strain DS2-3R

European journal of biochemistry, Aug 15, 1997

Research paper thumbnail of In vitro hydrogen production by glucose dehydrogenase and hydrogenase

Nature Biotechnology, Jul 1, 1996

A new in vitro enzymatic pathway for the generation of molecular hydrogen from glucose has been d... more A new in vitro enzymatic pathway for the generation of molecular hydrogen from glucose has been demonstrated. The reaction is based on the oxidation of glucose by Thermoplasma acidophilum glucose dehydrogenase with the concomitant oxidation of NADPH by Pyrococcus furiosus hydrogenase. Stoichiometric yields of hydrogen were produced from glucose with the continuous recycling of cofactor. This simple system may provide a method for the biological production of hydrogen from renewable sources. In addition, the other product of this reaction, gluconic acid, is a high-value chemical commodity.

Research paper thumbnail of Functional groups in the catalysis and regulation of Escherichia coli citrate synthase

Biochemical journal. Cellular aspects, Nov 1, 1972

Research paper thumbnail of Crystal structure of an Acetylating Aldehyde Dehydrogenase from Geobacillus thermoglucosidasius

Research paper thumbnail of Structure of Bacillus subtilis citrate synthase

Log In