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Coenzyme F420
Coenzyme F420 or 8-hydroxy-5-deazaflavin is a coenzyme (sometimes called a cofactor) involved in redox reactions in methanogens, in many Actinomycetota, and sporadically in other bacterial lineages. It is a flavin derivative. The coenzyme is a substrate for coenzyme F420 hydrogenase, 5,10-methylenetetrahydromethanopterin reductase and methylenetetrahydromethanopterin dehydrogenase. A particularly rich natural source of F420 is ''Mycobacterium smegmatis'', in which several dozen enzymes use F420 instead of the related cofactor FMN used by homologous enzymes in most other species. Eukaryotes including the fruit fly ''Drosophila melanogaster'' and the algae ''Ostreococcus tauri'' also use a precursor to this cofactor. Biosynthesis Coenzyme F420 is synthesized via a multi-step pathway: * 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase produces Coenzyme FO (also written F0), itself a cofactor of DNA photolyase (antenna). This is the head portion of the molecule. * 2-phos ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
F420
F420 may refer to : * Coenzyme F420, a coenzyme involved in redox reactions in methanogens * HMNZS Tutira (F420), a 1948 Loch class frigate of the Royal New Zealand Navy {{Letter-NumberCombDisambig ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ostreococcus Tauri
''Ostreococcus tauri'' is a unicellular species of marine green alga about 0.8 micrometres (μm) in diameter, the smallest free-living (non-symbiotic) eukaryote yet described. It has a very simple ultrastructure, and a compact genome. As a common member of global oceanic picoplankton populations, this organism has a major role in the carbon cycle in many areas. Recently, ''O. tauri'' has been the subject of studies using comparative genomics and functional genomics, as it is of interest to researchers because of its compact genome and green lineage. History ''Ostreococcus tauri'' was discovered in 1994 in the Thau lagoon, France, in a year-long study of the picoplankton population of the lagoon using flow cytometry. ''O. tauri'' was found to be the main component of the picoplankton population in the lagoon, and images of cells produced by transmission electron microscopy revealed the smallest yet described free-living eukaryotic cells. ''O. tauri'' was immediately placed in th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tetrahydromethanopterin
Tetrahydromethanopterin (THMPT, ) is a coenzyme in methanogenesis. It is the carrier of the C1 group as it is reduced to the methyl level, before transferring to the coenzyme M. Tetrahydrosarcinapterin (THSPT, ) is a modified form of THMPT, wherein a glutamyl group linked to the 2-hydroxyglutaric acid terminus. THMPT is the main platform for C1 transformations N-Formylmethanofuran donates the C1 group to the N5 site of the pterin to give the formyl- THMPT. The formyl group subsequently condenses intramolecularly to give methenyl- , which is then reduced to methylene- THMPT. Methylene- MPT is subsequently converted, using coenzyme F420 as the electron source, to methyl- THMPT, catalyzed by F420-dependent methylene-THMPT reductase. Methyl- THMPT is the methyl donor to coenzyme M, a conversion mediated by methyl-THMPT:coenzyme M methyltransferase. Comparison with tetrahydrofolic acid THMPT is related to the better known tetrahydrofolic acid (THFA, ). The most important d ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Methanofuran
Methanofurans are a family of chemical compounds found in methanogenic archaea. These species feature a 2-aminomethylfuran linked to phenoxy group. At least three different end groups are recognized: R = tricarboxyheptanoyl (methanofuran), glutamyl-glutamyl (methanofuran b), tricarboxy-2-hydroxyheptanoyl (methanofuran c, see picture). Formylation of MFR Methanofuran converts to formylmethanofuran in an early stage of methanogenesis. The enzyme formylmethanofuran dehydrogenase ( EC: 1.2.99.5) formylates methanofuran using , the primary C1 source in methanogenesis. Deformylation of MFR The enzyme formylmethanofuran:tetrahydromethanopterin formyltransferase catalyzes the transfer of the formyl group from formylmethanofuran to N5 on tetrahydromethanopterin, . This enzyme has been crystallized; it contains no prosthetic group A prosthetic group is the non-amino acid component that is part of the structure of the heteroproteins or conjugated proteins, being tightly linked to t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Coenzyme B
Coenzyme B is a coenzyme required for redox reactions in methanogens. The full chemical name of coenzyme B is 7-mercaptoheptanoylthreoninephosphate. The molecule contains a thiol, which is its principal site of reaction. Coenzyme B reacts with 2-methylthioethanesulfonate (methyl-Coenzyme M, abbreviated ), to release methane in methanogenesis: : + HS–CoB → + CoB–S–S–CoM This conversion is catalyzed by the enzyme methyl coenzyme M reductase, which contains cofactor F430 as the prosthetic group. A related conversion that utilizes both HS-CoB and HS-CoM is the reduction of fumarate to succinate, catalyzed by fumarate reductase Fumarate reductase is the enzyme that converts fumarate to succinate, and is important in microbial metabolism as a part of anaerobic respiration. Succinate + acceptor fumarate + reduced acceptor Fumarate reductases can be divided into two classe ...: :HS–CoM + HS–CoB + − → − + CoB–S–S–CoM Importance of Coenzyme B in Metha ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Coenzyme M
Coenzyme M is a coenzyme required for methyl-transfer reactions in the metabolism of archaeal methanogens, and in the metabolism of other substrates in bacteria. It is also a necessary cofactor in the metabolic pathway of alkene-oxidizing bacteria. CoM helps eliminate the toxic epoxides formed from the oxidation of alkenes such as propylene. The structure of this coenzyme was discovered by CD Taylor and RS Wolfe in 1974 while they were studying methanogenesis, the process by which carbon dioxide is transformed into methane in some anaerobic bacteria. The coenzyme is an anion with the formula . It is named 2-mercaptoethanesulfonate and abbreviated HS–CoM. The cation is unimportant, but the sodium salt is most available. Mercaptoethanesulfonate contains both a thiol, which is the main site of reactivity, and a sulfonate group, which confers solubility in aqueous media. Biochemical role Methanogenesis The coenzyme is the C1 donor in methanogenesis. It is converted to methyl-c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
L-glutamate Ligase
Glutamic acid (symbol Glu or E; the ionic form is known as glutamate) is an α-amino acid that is used by almost all living beings in the biosynthesis of proteins. It is a non-essential nutrient for humans, meaning that the human body can synthesize enough for its use. It is also the most abundant excitatory neurotransmitter in the vertebrate nervous system. It serves as the precursor for the synthesis of the inhibitory gamma-aminobutyric acid (GABA) in GABA-ergic neurons. Its molecular formula is . Glutamic acid exists in three optically isomeric forms; the dextrorotatory -form is usually obtained by hydrolysis of gluten or from the waste waters of beet-sugar manufacture or by fermentation.Webster's Third New International Dictionary of the English Language Unabridged, Third Edition, 1971. Its molecular structure could be idealized as HOOC−CH()−()2−COOH, with two carboxyl groups −COOH and one amino group −. However, in the solid state and mildly acidic water solutio ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
2-phospho-L-lactate Transferase
2-phospho-L-lactate transferase (, ''LPPG:Fo 2-phospho-L-lactate transferase'', ''LPPG:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase'', ''MJ1256'', ''lactyl-2-diphospho-(5')guanosine:Fo 2-phospho-L-lactate transferase'', ''CofD'') is an enzyme with systematic name ''(2S)-lactyl-2-diphospho-5'-guanosine:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase''. This enzyme catalyses the following chemical reaction : (2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin \rightleftharpoons GMP + coenzyme F420-0 This enzyme is involved in the biosynthesis of coenzyme F420 Coenzyme F420 or 8-hydroxy-5-deazaflavin is a coenzyme (sometimes called a cofactor) involved in redox reactions in methanogens, in many Actinomycetota, and sporadically in other bacterial lineages. It is a flavin derivative. The coenzyme is a .... References External links * {{Portal bar, Biology, border=no EC 2.7.8 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DNA Photolyase N-terminal Domain
DNA photolyase, N-terminal is an evolutionary conserved protein domain. This domain binds a light harvesting chromophore that enhanced the spectrum of photolyase or cryptochrome light absorption, i.e. an antenna. It adopts the rossmann fold. The cofactor may be either the pterin 5,10-Methenyltetrahydrofolate (MTHF, ) in ''folate photolyases'' () or the deazaflavin 8-hydroxy-7,8-didemethyl-5-deazariboflavin (8-HDF, ) in ''deazaflavin photolyases'' (). The 8-HDF ligand usually binds into this domain (next to the C-terinal half), while MHF tends to bind to an outside groove of this domain. A structural signature for 8-HDF binding has been produced, highlighting amino acid residues that determine which antenna a photolyase can use. Experiments on a ''Thermus thermophilus'' protein with this domain () shows that artificial substrates can be alternatively used for a modified absorption spectra. It naturally binds FMN in a pose similar to 8-HDF. In addition, many cryptochromes, especia ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
7,8-didemethyl-8-hydroxy-5-deazariboflavin Synthase
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase (, ''FO synthase'') and 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-hydroxyphenyl transferase () are two enzymes always complexed together to achieve synthesis of FO, a precursor to Coenzyme F420. Their systematic names are ''5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil ammonia-lyase (7,8-didemethyl-8-hydroxy-5-deazariboflavin-forming)'' and ''5-amino-6-(D-ribitylamino)uracil:L-tyrosine, 4-hydroxyphenyl transferase'' respectively. The enzymes catalyse the following chemical reactions: : (2.5.1.147) 5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosin : (4.3.1.32) 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 7,8-didemethyl-8-hydroxy-5-deazariboflavin + NH3 + L-methionine + 5'-deoxyadenosine Enzyme 2.5.1.147 binds a 4Fe-4S cl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Drosophila Melanogaster
''Drosophila melanogaster'' is a species of fly (the taxonomic order Diptera) in the family Drosophilidae. The species is often referred to as the fruit fly or lesser fruit fly, or less commonly the "vinegar fly" or "pomace fly". Starting with Charles W. Woodworth's 1901 proposal of the use of this species as a model organism, ''D. melanogaster'' continues to be widely used for biological research in genetics, physiology, microbial pathogenesis, and life history evolution. As of 2017, five Nobel Prizes have been awarded to drosophilists for their work using the insect. ''D. melanogaster'' is typically used in research owing to its rapid life cycle, relatively simple genetics with only four pairs of chromosomes, and large number of offspring per generation. It was originally an African species, with all non-African lineages having a common origin. Its geographic range includes all continents, including islands. ''D. melanogaster'' is a common pest in homes, restaurants, and othe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
