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carbon-sulfur lyases - metabolism (425) 425
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Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 31, pp. 12744 - 12753
Fe-S cofactors are composed of iron and inorganic sulfur in various stoichiometries. A complex assembly pathway conducts their initial synthesis and subsequent... 
HSPA9 | iron-response element (IRE) | mitochondrial respiratory chain complex | RESPIRATORY-CHAIN | ELEMENT-BINDING-PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | FE-S CLUSTERS | ESCHERICHIA-COLI | HSC20 | metalloenzyme | HEAVY-SUBUNIT | RESPONSIVE ELEMENT | CYSTEINE DESULFURASE | MESSENGER-RNA | iron-sulfur protein | iron-sulfur cluster biogenesis | SCAFFOLD PROTEIN | TARGETED DELETION | energy metabolism | ISCU | Iron Regulatory Protein 1 - physiology | Electron Transport | Humans | Protein Multimerization | Homeostasis | Succinate Dehydrogenase - biosynthesis | Iron-Binding Proteins - chemistry | Iron-Regulatory Proteins - biosynthesis | Succinate Dehydrogenase - chemistry | Iron-Sulfur Proteins - chemistry | Molecular Chaperones - chemistry | Apoenzymes - metabolism | Iron-Regulatory Proteins - physiology | Iron-Regulatory Proteins - chemistry | Iron-Sulfur Proteins - biosynthesis | Carbon-Sulfur Lyases - physiology | HSP70 Heat-Shock Proteins - chemistry | Protein Interaction Domains and Motifs | HSP70 Heat-Shock Proteins - biosynthesis | Molecular Chaperones - biosynthesis | Iron-Binding Proteins - physiology | Response Elements | Iron Regulatory Protein 1 - chemistry | Carbon-Sulfur Lyases - biosynthesis | Mitochondrial Proteins - physiology | Models, Molecular | Mitochondrial Proteins - biosynthesis | Molecular Chaperones - physiology | Iron-Binding Proteins - biosynthesis | Protein Folding | Iron-Sulfur Proteins - physiology | Gene Expression Regulation, Enzymologic | Animals | Iron - physiology | Mitochondrial Proteins - chemistry | Apoenzymes - chemistry | HSP70 Heat-Shock Proteins - physiology | Succinate Dehydrogenase - physiology | Carbon-Sulfur Lyases - chemistry | Iron Regulatory Protein 1 - biosynthesis | Minireviews
Journal Article
ChemBioChem, ISSN 1439-4227, 01/2015, Volume 16, Issue 1, pp. 100 - 109
CalE6 is a previously uncharacterized protein involved in the biosynthesis of calicheamicins in Micromonospora echinospora. It is a... 
protein structures | enzyme catalysis | methionine gamma‐lyase | calicheamicins | biosynthesis | Methionine gamma-lyase | Biosynthesis | Enzyme catalysis | Protein structures | Calicheamicins | ANTITUMOR ANTIBIOTICS | CHEMISTRY, MEDICINAL | METHYL MERCAPTAN | ACTIVE-SITE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | FAMILY | SYNTHASE | ENZYME | PURIFICATION | methionine gamma-lyase | PYRIDOXAL-PHOSPHATE | MENAQUINONE | Pyridoxal Phosphate - chemistry | Butyrates - metabolism | Multigene Family | Bacterial Proteins - chemistry | Molecular Sequence Data | Crystallography, X-Ray | Holoenzymes - chemistry | Carbon-Oxygen Lyases - chemistry | Pyridoxal Phosphate - metabolism | Coenzymes - metabolism | Sulfhydryl Compounds - metabolism | Holoenzymes - metabolism | Carbon-Sulfur Lyases - genetics | Micromonospora - genetics | Micromonospora - enzymology | Sulfhydryl Compounds - chemistry | Coenzymes - chemistry | Amino Acid Sequence | Catalytic Domain | Gene Expression | Methionine - metabolism | Bacterial Proteins - genetics | Models, Molecular | Enediynes | Carbon-Sulfur Lyases - metabolism | Sequence Homology, Amino Acid | Sequence Alignment | Ammonium Compounds - metabolism | Methionine - chemistry | Butyrates - chemistry | Carbon-Oxygen Lyases - genetics | Aminoglycosides - biosynthesis | Carbon-Oxygen Lyases - metabolism | Bacterial Proteins - metabolism | Holoenzymes - genetics | Carbon-Sulfur Lyases - chemistry | Ammonium Compounds - chemistry
Journal Article
Journal Article
IUBMB Life, ISSN 1521-6543, 09/2017, Volume 69, Issue 9, pp. 668 - 676
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 01/2015, Volume 290, Issue 1, pp. 671 - 681
Journal Article
Nature Communications, ISSN 2041-1723, 12/2017, Volume 8, Issue 1, pp. 1287 - 15
Iron-sulfur (Fe/S) clusters are essential protein cofactors crucial for many cellular functions including DNA maintenance, protein translation, and energy... 
IRON-SULFUR CLUSTER | ACYL CARRIER PROTEIN | CYSTEINE DESULFURASE | FRATAXIN | ARABIDOPSIS-THALIANA | BIOGENESIS | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | X-RAY | SCAFFOLD PROTEIN | Fungal Proteins - chemistry | Humans | Protein Multimerization | Iron-Sulfur Proteins - genetics | Crystallography, X-Ray | Iron-Binding Proteins - chemistry | Mitochondrial Proteins - genetics | Iron-Sulfur Proteins - chemistry | Iron-Binding Proteins - metabolism | Multiprotein Complexes - metabolism | Carbon-Sulfur Lyases - genetics | Mitochondrial Proteins - metabolism | X-Ray Diffraction | Iron-Regulatory Proteins - chemistry | Protein Stability | Amino Acid Sequence | Chaetomium - chemistry | Mutagenesis, Site-Directed | Acyl Carrier Protein - metabolism | Models, Molecular | Scattering, Small Angle | Iron-Regulatory Proteins - metabolism | Mitochondria - metabolism | Fungal Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Static Electricity | Carbon-Sulfur Lyases - metabolism | Chaetomium - genetics | Iron-Regulatory Proteins - genetics | Molecular Dynamics Simulation | Sequence Homology, Amino Acid | Acyl Carrier Protein - chemistry | Multiprotein Complexes - chemistry | Acyl Carrier Protein - genetics | Mitochondrial Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Iron-Binding Proteins - genetics | Protein Conformation | Iron-Sulfur Proteins - metabolism | Carbon-Sulfur Lyases - chemistry | Amino Acid Substitution | Fungal Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Iron | Small angle X ray scattering | Crystallography | Cofactors | Proteins | Energy balance | Mitochondria | X-ray scattering | Frataxin | Energy conversion | Acyl carrier protein | Clusters | X ray scattering | Catalysis | Ferredoxin | Sulfur | Chemical synthesis | Deoxyribonucleic acid--DNA | Crystal structure | Lipids
Journal Article
Biochemical Journal, ISSN 0264-6021, 07/2017, Volume 474, Issue 14, pp. 2435 - 2447
Journal Article