Molybdopterin
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| Surname | Molybdopterin | |||||||||
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| Molecular formula | C 10 H 14 N 5 O 6 PS 2 | |||||||||
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| Molar mass | 395.32 g mol −1 (R = H) | |||||||||
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firmly |
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| As far as possible and customary, SI units are used. Unless otherwise noted, the data given apply to standard conditions . | ||||||||||
Molybdopterin is a chemical compound that builds up on a pterin ring . Together with a molybdenum ion, molybdopterin forms the molybdenum cofactor (MoCo).
properties
Molybdopterin consists of a pyranopterin, a heterocycle of a pyran ring and a pteridine ring . There are two thiolates on the pyran ring . In some cases the alkyl phosphate group is an alkyl diphosphate nucleotide group (from adenosine diphosphate ).
Different enzymes use molybdopterin. Molybdopterin is a cofactor of xanthine oxidase , DMSO reductase , sulfite oxidase , nitrate reductase , ethylbenzene dehydrogenase , glyceraldehyde-3-phosphate ferredoxin oxidoredrogenuctase , arsenate reductase (glutaredoxin) and carbon monoxide dehydrogenase . Furthermore, molybdopterin is a prosthetic group of various enzymes such as formate dehydrogenase , purine hydroxylase and thiosulfate reductase . Molybdopterin also occurs in aldehyde oxidase .
In some types of bacteria, tungstate is bound to molybdopterin instead of molybdate in their oxidoreductases . These enzymes mostly oxidize aldehydes to carboxylic acids . Some tungstate-binding oxidoreductases use selenium instead of sulfur.
biosynthesis
Molybdopterin is synthesized from guanosine triphosphate . Pyranopterin is formed in the first intermediate step via a radical reaction with S-adenosylmethionine . An endithiolate is then formed in three further reaction steps . The phosphate group is coupled to adenosine diphosphate , which creates molybdopterin.
The models of the active centers of molybdopterin-containing enzymes are derived from dithiolene-containing ligands .
Individual evidence
- ↑ This substance has either not yet been classified with regard to its hazardousness or a reliable and citable source has not yet been found.
- ↑ a b c Structure, synthesis, empirical formula for the di-sulfhydryl. Accessed Nov. 16, 2009.
- ↑ Katharina Munk (ed.): Pocket textbook biology. Biochemistry - Cell Biology. ( limited preview in Google Book search) . Georg Thieme, Stuttgart 2008, ISBN 978-3-13-144831-6 .
- ^ Erik Lassner: Tungsten: Properties, Chemistry, Technology of the Element, Alloys and Chemical Compounds. Springer Science & Business Media, 1999, ISBN 978-0-306-45053-2 , p. 409 ( limited preview in Google book search).
- ↑ Stiefel, EI: Transition metal sulfur chemistry and its relevance to molybdenum and tungsten enzymes . In: Pure Appl. Chem. . 70, No. 4, 1998, pp. 889-896. doi : 10.1351 / pac199870040889 .
- ↑ Schräder T, Rienhöfer A, Andreesen JR: Selenium-containing xanthine dehydrogenase from Eubacterium barkeri . In: Eur. J. Biochem . 264, No. 3, September 1999, pp. 862-71. doi : 10.1046 / j.1432-1327.1999.00678.x . PMID 10491134 .
- ↑ Schwarz, G. and Mendel, RR: Molybdenum cofactor biosynthesis and molybdenum enzymes . In: Annu. Rev. Plant Biol . 57, 2006, pp. 623-647. doi : 10.1146 / annurev.arplant.57.032905.105437 . PMID 16669776 .
- ↑ Kisker, C .; Schindelin, H .; Baas, D .; Rétey, J .; Meckenstock, RU; Kroneck, PMH: A structural comparison of molybdenum cofactor-containing enzymes . In: FEMS Microbiol. Rev . 22, No. 5, 1999, pp. 503-521. doi : 10.1111 / j.1574-6976.1998.tb00384.x . PMID 9990727 .