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shewanella - enzymology (327) 327
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Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/2007, Volume 104, Issue 2, pp. 473 - 478
Tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) constitute an important, yet relatively poorly understood, family of heme-containing... 
Proteins | Enzymes | Molecules | Active sites | Atomic interactions | Atoms | Biochemistry | Catalysis | Monomers | Enzyme substrates | Indoleamine 2,3-dioxygenase | Immunomodulation | Heme enzymes | Cancer | immunomodulation | heme enzymes | CATABOLISM | KYNURENINE PATHWAY | CRYSTAL-STRUCTURE | TOLERANCE | MULTIDISCIPLINARY SCIENCES | REPLACEMENT | DEGRADATION | DIFFRACTION | cancer | HUMAN INDOLEAMINE 2,3-DIOXYGENASE | indoleamine 2,3-dioxygenase | EXPRESSION | PROGRAM | Indoleamine-Pyrrole 2,3,-Dioxygenase - genetics | Indoleamine-Pyrrole 2,3,-Dioxygenase - metabolism | Indoleamine-Pyrrole 2,3,-Dioxygenase - chemistry | Humans | Molecular Sequence Data | Substrate Specificity | Xanthomonas campestris - genetics | Crystallography, X-Ray | Protein Structure, Quaternary | Xanthomonas campestris - enzymology | Recombinant Proteins - metabolism | Amino Acid Sequence | Shewanella - genetics | Shewanella - enzymology | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Static Electricity | Sequence Homology, Amino Acid | Tryptophan Oxygenase - metabolism | Tryptophan Oxygenase - genetics | Hydrogen Bonding | Tryptophan Oxygenase - chemistry | Allosteric Site | Protein Conformation | Kinetics | In Vitro Techniques | Substrates (Biochemistry) | Research | Tryptophan metabolism | Heme | Biological Sciences
Journal Article
Applied and Environmental Microbiology, ISSN 0099-2240, 11/2007, Volume 73, Issue 21, pp. 7003 - 7012
Journal Article
Journal Article
Journal Article
MicrobiologyOpen, ISSN 2045-8827, 02/2016, Volume 5, Issue 1, pp. 21 - 38
We recently reported a flavin‐trafficking protein (Ftp) in the syphilis spirochete Treponema pallidum (Ftp_Tp) as the first bacterial metal‐dependent FAD... 
FAD pyrophosphatase | lipoprotein | flavoprotein | FMN transferase | posttranslational modification | redox protein | Posttranslational modification | Flavoprotein | Lipoprotein | Redox protein | CRYSTAL-STRUCTURE | FLAVODOXINS | MICROBIOLOGY | TREPONEMA-PALLIDUM | REDUCTION | THIAMINE SYNTHESIS | BIOSYNTHESIS | SEQUENCE | BINDING | CHOLERAE | Escherichia coli - enzymology | Flavoproteins - metabolism | Mutagenesis, Site-Directed | Oxidation-Reduction | Periplasm - enzymology | Adenosine Monophosphate - metabolism | Pyrophosphatases - genetics | Shewanella - enzymology | Crystallography, X-Ray | Shewanella - metabolism | Protein Transport | Pyrophosphatases - metabolism | Flavin-Adenine Dinucleotide - metabolism | Periplasm - metabolism | Escherichia coli - metabolism | Bacterial Proteins - metabolism | Protein Processing, Post-Translational | Flavin Mononucleotide - metabolism | Flavoproteins - biosynthesis | Sexually transmitted diseases--STD | Metals | Homeostasis | Biosynthesis | Amino acid substitution | Proteins | E coli | Bioenergetics | Syphilis | Bacteria | Catalysis | Magnesium | Protein transport | Pyrophosphatase | Deoxyribonucleic acid--DNA | Crystal structure | AMP | Globus pallidus | Metabolism | Substrates | Exports | Flavin-adenine dinucleotide | Studies | Bimetals | Flavin mononucleotide | Mutagenesis | Lysine | Periplasm | Flavoproteins | Index Medicus
Journal Article