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TitleStructure-function analyses of alkylhydroperoxidase D from Streptococcus pneumoniae reveal an unusual three-cysteine active site architecture
Publication TypeJournal Article
Year of Publication2020
AuthorsMeng, Y., Sheen C.R., Magon N.J., Hampton M.B., and Dobson R.C.J.
JournalJournal of Biological Chemistry
Pagination2984 - 2999
Date Published2020
KeywordsActive site architecture, Amino Acid Motifs, amino acid sequence, Amino acids, anaerobic growth, article, bacterial protein, Bacterial Proteins, biocatalysis, catalase, Catalytic Domain, chemistry, Chromatography, High Pressure Liquid, controlled study, Covalent bonds, crystal structure, Crystallography, X-Ray, cysteine, dimerization, disulfide, Disulfides, Dithiothreitol, Electron transitions, electron transport, enzyme active site, enzyme activity, enzyme structure, Enzymes, enzymology, Facultative anaerobes, genetics, Gram negative bacterium, Gram positive bacterium, high performance liquid chromatography, Hydrogen peroxide, in vivo study, lactate 2 monooxygenase, liquid chromatography, Mass spectrometry, metabolism, Millimolar concentrations, Mutagenesis, Site-Directed, Mycobacterium tuberculosis, nonhuman, Oxidation, oxidation reduction state, oxidative stress, Oxidative stress response, oxidoreductase, peroxidase, Peroxidase activities, Peroxidases, Peroxides, priority journal, protein motif, protein quaternary structure, protein structure, Protein Structure, Quaternary, pyruvic acid, reduced nicotinamide adenine dinucleotide dehydrogenase, sequence alignment, site directed mutagenesis, Streptococcus pneumoniae, Structure-function analysis, Sulfur compounds, superoxide dismutase, tandem mass spectrometry, Thiol, ultracentrifugation, X ray crystallography, X ray diffraction

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