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Substrate Orientation and Specificity in Xanthine Oxidase: Crystal Structures of the Enzyme in Complex with Indole-3-acetaldehyde and Guanine
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1016/0014-5793(81)80406-1openalex-snapshot
Purification of highly active milk xanthine oxidase by affinity chromatography on sepharose 4B/folate gel
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Molybdenum-containing hydroxylases
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Molybdenum enzymes in higher organisms
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The reductive half-reaction of xanthine oxidase. Identification of spectral intermediates in the hydroxylation of 2-hydroxy-6-methylpurine.
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On the mechanism of action of xanthine oxidase. Evidence in support of an oxo transfer mechanism in the molybdenum-containing hydroxylases.
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Studies on Milk Xanthine Oxidase
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The Reaction of Xanthine Oxidase with Molecular Oxygen
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Kinetic Studies on the Substrate Reduction of Xanthine Oxidase
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Modern developments in molecular replacement
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Comparison of Formation of Reactive Conformers (NACs) for the Claisen Rearrangement of Chorismate to Prephenate in Water and in the E. c oli Mutase: The Efficiency of the Enzyme Catalysis
inferredcites →https://doi.org/10.1021/ja027388dopenalex-snapshot
The Reaction Mechanism of Xanthine Oxidase: Evidence for Two-Electron Chemistry Rather Than Sequential One-Electron Steps
inferredcites →https://doi.org/10.1021/ja0293047openalex-snapshot
Enzymes Do What Is Expected (Chalcone Isomerase versus Chorismate Mutase)
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The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme
inferredcites →https://doi.org/10.1073/pnas.93.17.8846openalex-snapshot
A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes.
inferredcites →https://doi.org/10.1073/pnas.97.20.10723openalex-snapshot
Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion
inferredcites →https://doi.org/10.1074/jbc.271.12.6771openalex-snapshot
The Reductive Half-reaction of Xanthine Oxidase
inferredcites →https://doi.org/10.1074/jbc.274.6.3323openalex-snapshot
The Reductive Half-reaction of Xanthine Oxidase
inferredcites →https://doi.org/10.1074/jbc.m110.128561openalex-snapshot
Substrate Orientation and Catalytic Specificity in the Action of Xanthine Oxidase
inferredcites →https://doi.org/10.1074/jbc.m112.390419openalex-snapshot
The First Mammalian Aldehyde Oxidase Crystal Structure
inferredcites →https://doi.org/10.1074/jbc.m405778200openalex-snapshot
The Role of Active Site Glutamate Residues in Catalysis of Rhodobacter capsulatus Xanthine Dehydrogenase
inferredcites →https://doi.org/10.1074/jbc.m700364200openalex-snapshot
The Role of Arginine 310 in Catalysis and Substrate Specificity in Xanthine Dehydrogenase from Rhodobacter capsulatus
inferredcites →https://doi.org/10.1074/jbc.m707918200openalex-snapshot
Substrate Orientation in Xanthine Oxidase
inferredcites →https://doi.org/10.1074/jbc.m804517200openalex-snapshot
Substrate Orientation and Catalysis at the Molybdenum Site in Xanthine Oxidase
inferredcites →https://doi.org/10.1074/jbc.m808114200openalex-snapshot
Mechanism of Substrate and Inhibitor Binding of Rhodobacter capsulatus Xanthine Dehydrogenase
inferredcites →https://doi.org/10.1093/jb/mvm053openalex-snapshot
Human Xanthine Oxidase Changes its Substrate Specificity to Aldehyde Oxidase Type upon Mutation of Amino Acid Residues in the Active Site: Roles of Active Site Residues in Binding and Activation of Purine Substrate
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Overview of the CCP 4 suite and current developments
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Refinement of Macromolecular Structures by the Maximum-Likelihood Method
inferredcites →https://doi.org/10.1107/s0907444998004119openalex-snapshot
Incorporation of Prior Phase Information Strengthens Maximum-Likelihood Structure Refinement
inferredcites →https://doi.org/10.1107/s090744499801405xopenalex-snapshot
Efficient anisotropic refinement of macromolecular structures using FFT
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Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Additional file 1 of Potential natural inhibitors of xanthine oxidase and HMG-CoA reductase in cholesterol regulation: in silico analysis
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