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International Journal of Biological Macromolecules, ISSN 0141-8130, 10/2019, Volume 138, pp. 986 - 995
FAD synthase, the last enzyme of the pathway converting riboflavin to FAD, exists in humans in different isoforms, with isoforms 1, 2 and 6 being characterized... 
NAD | FAD | FAD hydrolysis | Molybdopterin-binding domain | Human FAD synthase | RAT-LIVER | POLYMER SCIENCE | PYROPHOSPHATASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MITOCHONDRIA | FMN PHOSPHOHYDROLASE | ACYL-COA DEHYDROGENASE | METABOLISM | NAD(+) | OVER-EXPRESSION | NUDIX HYDROLASE | CHEMISTRY, APPLIED | FLAVIN ADENINE-DINUCLEOTIDE | Physiological aspects | Enzymes | Fluorides | Catalysis | Molybdenum compounds
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 07/2018, Volume 502, Issue 1, pp. 48 - 54
Molybdenum cofactor (Moco), molybdopterin (MPT) complexed with molybdenum, is an essential cofactor required for the catalytic center of diverse enzymes in all... 
Molybdopterin synthase | MoaD | MoaE | Deinococcus radiodurans | JAMM/MPN+ metalloprotease | metalloprotease | JAMM/MPN | MYCOBACTERIUM-TUBERCULOSIS | BIOPHYSICS | ENZYMES | BIOCHEMISTRY & MOLECULAR BIOLOGY | UBIQUITIN-LIKE PROTEIN
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 09/2015, Volume 465, Issue 3, pp. 443 - 449
Journal Article
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, ISSN 1422-0067, 12/2012, Volume 13, Issue 12, pp. 16880 - 16898
FAD synthase (FADS, EC 2.7.7.2) is a key enzyme in the metabolic pathway that converts riboflavin into the redox cofactor, FAD. Human FADS is organized in two... 
MECHANISM | MOLYBDENUM | ESCHERICHIA-COLI | FAD | human FAD synthase | STRUCTURAL GENE | SACCHAROMYCES-CEREVISIAE | CHEMISTRY, MULTIDISCIPLINARY | Flavin | METABOLISM | FLAD1 | BIOSYNTHESIS | SYNTHETASE | FMN adenylyltransferase | FLAVOKINASE | molybdopterin-binding domain | PAPS reductase domain | FLAVIN ADENINE-DINUCLEOTIDE
Journal Article
Critical Reviews in Biochemistry and Molecular Biology, ISSN 1040-9238, 2004, Volume 39, Issue 3, pp. 165 - 195
This review focuses on how microbes live on CO as a sole source of carbon and energy and with CO by generating carbon monoxide as a metabolic intermediate. The... 
iron-sulfur cluster | corrinoid protein | acetyl-CoA synthase | methanogenesis | carbon dioxide fixation | pyruvate ferredoxin oxidoreductase | metallobiochemistry | iron-sulfur | copper | molybdopterin | pyruvate synthase | anaerobe | EPR spectroscopy | autotrophic growth | nickel | methyltransferase | CO dehydrogenase | vitamin B | heme | Wood-Ljungdahl pathway | evolution | metalloenzyme | IR spectroscopy | acetogenesis | folate | gene regulation | fixation | substrate channeling | vitamin B12 | CO2 fixation | CH3-H4folate | Gene regulation | Acetogenesis | Iron-sulfur cluster | Metalloenzyme | Metallobiochemistry | Iron-sulfur | Carbon dioxide fixation | Heme | Methanogenesis | Evolution | Molybdopterin | Nickel | Copper | Acetyl-CoA synthase | METHYL-GROUP TRANSFER | SENSING TRANSCRIPTIONAL ACTIVATOR | RAY-ABSORPTION-SPECTROSCOPY | ELECTRON-PARAMAGNETIC-RES | PYRUVATE-FERREDOXIN OXIDOREDUCTASE | COENZYME-A SYNTHASE | IRON-SULFUR PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | FREE-RADICAL INTERMEDIATE | CH3-H-4 folate | vitamin B-12 | THERMOCARBOXYDOVORANS STRAIN C2 | Aldehyde Oxidoreductases - physiology | Acetate-CoA Ligase - chemistry | Bacteria, Aerobic - genetics | Bacteria, Anaerobic - enzymology | Bacteria, Anaerobic - genetics | Carbon Monoxide - metabolism | Multienzyme Complexes - chemistry | Bacteria, Aerobic - enzymology | Biological Transport, Active | Aldehyde Oxidoreductases - chemistry | Multienzyme Complexes - physiology | Protein Conformation | Bacteria, Anaerobic - metabolism | Acetate-CoA Ligase - physiology | Bacteria, Aerobic - metabolism
Journal Article
Biochemistry, ISSN 0006-2960, 09/2008, Volume 47, Issue 39, pp. 10354 - 10364
Journal Article
Progress in Lipid Research, ISSN 0163-7827, 2010, Volume 49, Issue 1, pp. 27 - 45
Journal Article