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14-416: F430 may refer to: Cofactor F430 , F 430 , the prosthetic group of the enzyme methyl coenzyme M reductase Farman F.430 , a 1930s French light transport aircraft designed and built by Farman Aviation Works Ferrari F430 , a supercar produced by Italian automaker Ferrari from 2004 to 2009 F430, French cloud rap band [REDACTED] Topics referred to by

28-412: A , c -diamide. The sequence of the two amidations is random. A two-component complex Ni-sirohydrochlorin a,c-diamide reductive cyclase (CfbCD) carries out a 6-electron and 7-proton reduction of the ring system in a reaction EC 6.3.3.7 generating the 15,17 - seco -F 430 -17 -acid ( seco -F 430 ) intermediate. Reduction involves ATP hydrolysis and electrons are relayed through two 4Fe-4S centres. In

42-488: Is converted to sirohydrochlorin via dihydrosirohydrochlorin . Insertion of nickel into this tetrapyrrole is catalysed in reaction EC 4.99.1.11 by the same chelatase , CbiX , which inserts cobalt in the biosynthesis of cobalamin , here giving nickel(II)-sirohydrochlorin. The ATP-dependent Ni-sirohydrochlorin a,c-diamide synthase (CfbE) then converts the a and c acetate side chains to acetamide in reactions EC 6.3.5.12 , generating nickel(II)-sirohydrochlorin

56-409: Is different from Wikidata All article disambiguation pages All disambiguation pages Cofactor F430 It is found only in methanogenic Archaea and anaerobic methanotrophic Archaea. It occurs in relatively high concentrations in archaea that are involved in reverse methanogenesis: these can contain up to 7% by weight of the nickel protein. The trivial name cofactor F 430

70-575: The EMBL-EBI Enzyme Portal). Before the development of the EC number system, enzymes were named in an arbitrary fashion, and names like old yellow enzyme and malic enzyme that give little or no clue as to what reaction was catalyzed were in common use. Most of these names have fallen into disuse, though a few, especially proteolyic enzymes with very low specificity, such as pepsin and papain , are still used, as rational classification on

84-598: The chemical reactions they catalyze . As a system of enzyme nomenclature , every EC number is associated with a recommended name for the corresponding enzyme-catalyzed reaction. EC numbers do not specify enzymes but enzyme-catalyzed reactions. If different enzymes (for instance from different organisms) catalyze the same reaction, then they receive the same EC number. Furthermore, through convergent evolution , completely different protein folds can catalyze an identical reaction (these are sometimes called non-homologous isofunctional enzymes ) and therefore would be assigned

98-452: The tripeptide aminopeptidases have the code "EC 3.4.11.4", whose components indicate the following groups of enzymes: NB:The enzyme classification number is different from the 'FORMAT NUMBER' Oxidation /reduction reactions; transfer of H and O atoms or electrons from one substance to another Similarity between enzymatic reactions can be calculated by using bond changes, reaction centres or substructure metrics (formerly EC-BLAST], now

112-550: The Enzyme Commission was dissolved at that time, though its name lives on in the term EC Number . The current sixth edition, published by the International Union of Biochemistry and Molecular Biology in 1992 as the last version published as a printed book, contains 3196 different enzymes. Supplements 1-4 were published 1993–1999. Subsequent supplements have been published electronically, at the website of

126-605: The basis of specificity has been very difficult. By the 1950s the chaos was becoming intolerable, and after Hoffman-Ostenhof and Dixon and Webb had proposed somewhat similar schemes for classifying enzyme-catalyzed reactions, the International Congress of Biochemistry in Brussels set up the Commission on Enzymes under the chairmanship of Malcolm Dixon in 1955. The first version was published in 1961, and

140-412: The final step, the keto-containing carbocyclic ring F is formed by an ATP-dependent enzyme Coenzyme F(430) synthetase (CfbB) in reaction EC 6.4.1.9 , generating coenzyme F 430 . This enzyme is a MurF-like ligase , as found in peptidoglycan biosynthesis. Enzyme Commission number The Enzyme Commission number ( EC number ) is a numerical classification scheme for enzymes , based on

154-401: The same EC number. By contrast, UniProt identifiers uniquely specify a protein by its amino acid sequence. Every enzyme code consists of the letters "EC" followed by four numbers separated by periods. Those numbers represent a progressively finer classification of the enzyme. Preliminary EC numbers exist and have an 'n' as part of the fourth (serial) digit (e.g. EC 3.5.1.n3). For example,

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168-449: The same term This disambiguation page lists articles associated with the same title formed as a letter–number combination. If an internal link led you here, you may wish to change the link to point directly to the intended article. Retrieved from " https://en.wikipedia.org/w/index.php?title=F430&oldid=1145919144 " Category : Letter–number combination disambiguation pages Hidden categories: Short description

182-407: The standard tetrapyrrole (rings A-D), having a γ-lactam ring E and a keto-containing carbocyclic ring F. It is the only natural tetrapyrrole containing nickel , an element rarely found in biological systems. The biosynthesis builds from uroporphyrinogen III , the progenitor of all natural tetrapyrroles, including chlorophyll, vitamin B 12 , phycobilins, siroheme, heme, and heme d 1 . It

196-521: Was assigned in 1978 based on the properties of a yellow sample extracted from Methanobacterium thermoautotrophicum , which had a spectroscopic maximum at 430 nm. It was identified as the MCR cofactor in 1982 and the complete structure was deduced by X-ray crystallography and NMR spectroscopy . Coenzyme F 430 features a reduced porphyrin in a macrocyclic ring system called a corphin. In addition, it possesses two additional rings in comparison to

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