The Experts below are selected from a list of 1224 Experts worldwide ranked by ideXlab platform
Inger Andersson - One of the best experts on this subject based on the ideXlab platform.
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clavulanic acid dehydrogenase structural and biochemical analysis of the final step in the biosynthesis of the beta lactamase inhibitor clavulanic acid
Biochemistry, 2007Co-Authors: Alasdair Mackenzie, Nadia J Kershaw, Helena Hernandez, Carol V Robinson, Christopher J Schofield, Inger AnderssonAbstract:The ultimate step in the biosynthesis of the medicinally important β-lactamase inhibitor clavulanic acid is catalyzed by clavulanic acid dehydrogenase (CAD). CAD is responsible for the NAPDH-dependent reduction of the unstable intermediate clavulanate-9-aldehyde to yield clavulanic acid. Here, we report biochemical and structural studies on CAD. Biophysical analyses demonstrate that CAD exists as dimeric and tetrameric species in solution. The reaction performed by CAD was shown to be reversible, allowing the use of clavulanic acid for activity analyses. The crystal structure of CAD was solved using single-wavelength anomalous diffraction with a seleno-Methionine Derivative. The structure reveals that the individual monomers comprise a single domain possessing the Rossmann fold, characteristic of dinucleotide-binding enzymes. The monomers are arranged as tetramers, similar to other tetrameric members of the short-chain dehydrogenase/reductase family. The structure of the unreactive complex of CAD with cla...
Alasdair Mackenzie - One of the best experts on this subject based on the ideXlab platform.
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clavulanic acid dehydrogenase structural and biochemical analysis of the final step in the biosynthesis of the beta lactamase inhibitor clavulanic acid
Biochemistry, 2007Co-Authors: Alasdair Mackenzie, Nadia J Kershaw, Helena Hernandez, Carol V Robinson, Christopher J Schofield, Inger AnderssonAbstract:The ultimate step in the biosynthesis of the medicinally important β-lactamase inhibitor clavulanic acid is catalyzed by clavulanic acid dehydrogenase (CAD). CAD is responsible for the NAPDH-dependent reduction of the unstable intermediate clavulanate-9-aldehyde to yield clavulanic acid. Here, we report biochemical and structural studies on CAD. Biophysical analyses demonstrate that CAD exists as dimeric and tetrameric species in solution. The reaction performed by CAD was shown to be reversible, allowing the use of clavulanic acid for activity analyses. The crystal structure of CAD was solved using single-wavelength anomalous diffraction with a seleno-Methionine Derivative. The structure reveals that the individual monomers comprise a single domain possessing the Rossmann fold, characteristic of dinucleotide-binding enzymes. The monomers are arranged as tetramers, similar to other tetrameric members of the short-chain dehydrogenase/reductase family. The structure of the unreactive complex of CAD with cla...
Xiangyu Yang - One of the best experts on this subject based on the ideXlab platform.
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preclinical evaluation of an 18 f trifluoroborate Methionine Derivative for glioma imaging
European Journal of Nuclear Medicine and Molecular Imaging, 2018Co-Authors: Xiangyu Yang, Zhibo Liu, Huimin Zhang, Jeeva Munasinghe, Gang Niu, Gaojun Teng, Xiaoyuan ChenAbstract:Purpose 11C–Methionine (MET) is one of the most commonly used amino acid tracers for PET imaging of brain tumors. In this study, we report an 18F-labeled boron-derived Methionine analogue, denoted as 18F-B-MET, as a potential substitute of 11C–MET for glioma PET imaging.
Helena Hernandez - One of the best experts on this subject based on the ideXlab platform.
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clavulanic acid dehydrogenase structural and biochemical analysis of the final step in the biosynthesis of the beta lactamase inhibitor clavulanic acid
Biochemistry, 2007Co-Authors: Alasdair Mackenzie, Nadia J Kershaw, Helena Hernandez, Carol V Robinson, Christopher J Schofield, Inger AnderssonAbstract:The ultimate step in the biosynthesis of the medicinally important β-lactamase inhibitor clavulanic acid is catalyzed by clavulanic acid dehydrogenase (CAD). CAD is responsible for the NAPDH-dependent reduction of the unstable intermediate clavulanate-9-aldehyde to yield clavulanic acid. Here, we report biochemical and structural studies on CAD. Biophysical analyses demonstrate that CAD exists as dimeric and tetrameric species in solution. The reaction performed by CAD was shown to be reversible, allowing the use of clavulanic acid for activity analyses. The crystal structure of CAD was solved using single-wavelength anomalous diffraction with a seleno-Methionine Derivative. The structure reveals that the individual monomers comprise a single domain possessing the Rossmann fold, characteristic of dinucleotide-binding enzymes. The monomers are arranged as tetramers, similar to other tetrameric members of the short-chain dehydrogenase/reductase family. The structure of the unreactive complex of CAD with cla...
Carol V Robinson - One of the best experts on this subject based on the ideXlab platform.
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clavulanic acid dehydrogenase structural and biochemical analysis of the final step in the biosynthesis of the beta lactamase inhibitor clavulanic acid
Biochemistry, 2007Co-Authors: Alasdair Mackenzie, Nadia J Kershaw, Helena Hernandez, Carol V Robinson, Christopher J Schofield, Inger AnderssonAbstract:The ultimate step in the biosynthesis of the medicinally important β-lactamase inhibitor clavulanic acid is catalyzed by clavulanic acid dehydrogenase (CAD). CAD is responsible for the NAPDH-dependent reduction of the unstable intermediate clavulanate-9-aldehyde to yield clavulanic acid. Here, we report biochemical and structural studies on CAD. Biophysical analyses demonstrate that CAD exists as dimeric and tetrameric species in solution. The reaction performed by CAD was shown to be reversible, allowing the use of clavulanic acid for activity analyses. The crystal structure of CAD was solved using single-wavelength anomalous diffraction with a seleno-Methionine Derivative. The structure reveals that the individual monomers comprise a single domain possessing the Rossmann fold, characteristic of dinucleotide-binding enzymes. The monomers are arranged as tetramers, similar to other tetrameric members of the short-chain dehydrogenase/reductase family. The structure of the unreactive complex of CAD with cla...