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The biosynthesis of the molybdenum cofactors

  • The biosynthesis of the molybdenum cofactors (Moco) is an ancient, ubiquitous, and highly conserved pathway leading to the biochemical activation of molybdenum. Moco is the essential component of a group of redox enzymes, which are diverse in terms of their phylogenetic distribution and their architectures, both at the overall level and in their catalytic geometry. A wide variety of transformations are catalyzed by these enzymes at carbon, sulfur and nitrogen atoms, which include the transfer of an oxo group or two electrons to or from the substrate. More than 50 molybdoenzymes were identified to date. In all molybdoenzymes except nitrogenase, molybdenum is coordinated to a dithiolene group on the 6-alkyl side chain of a pterin called molybdopterin (MPT). The biosynthesis of Moco can be divided into three general steps, with a fourth one present only in bacteria and archaea: (1) formation of the cyclic pyranopterin monophosphate, (2) formation of MPT, (3) insertion of molybdenum into molybdopterin to form Moco, and (4) additionalThe biosynthesis of the molybdenum cofactors (Moco) is an ancient, ubiquitous, and highly conserved pathway leading to the biochemical activation of molybdenum. Moco is the essential component of a group of redox enzymes, which are diverse in terms of their phylogenetic distribution and their architectures, both at the overall level and in their catalytic geometry. A wide variety of transformations are catalyzed by these enzymes at carbon, sulfur and nitrogen atoms, which include the transfer of an oxo group or two electrons to or from the substrate. More than 50 molybdoenzymes were identified to date. In all molybdoenzymes except nitrogenase, molybdenum is coordinated to a dithiolene group on the 6-alkyl side chain of a pterin called molybdopterin (MPT). The biosynthesis of Moco can be divided into three general steps, with a fourth one present only in bacteria and archaea: (1) formation of the cyclic pyranopterin monophosphate, (2) formation of MPT, (3) insertion of molybdenum into molybdopterin to form Moco, and (4) additional modification of Moco in bacteria with the attachment of a nucleotide to the phosphate group of MPT, forming the dinucleotide variant of Moco. This review will focus on the biosynthesis of Moco in bacteria, humans and plants.zeige mehrzeige weniger

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Metadaten
Verfasserangaben:Ralf R. Mendel, Silke LeimkühlerORCiDGND
DOI:https://doi.org/10.1007/s00775-014-1173-y
ISSN:0949-8257
ISSN:1432-1327
Pubmed ID:https://pubmed.ncbi.nlm.nih.gov/24980677
Titel des übergeordneten Werks (Englisch):Journal of biological inorganic chemistry
Verlag:Springer
Verlagsort:New York
Publikationstyp:Rezension
Sprache:Englisch
Jahr der Erstveröffentlichung:2015
Erscheinungsjahr:2015
Datum der Freischaltung:27.03.2017
Freies Schlagwort / Tag:Molybdenum; Molybdenum cofactor; Sulfite oxidase; Sulfuration; bis-MGD; cPMP
Band:20
Ausgabe:2
Seitenanzahl:11
Erste Seite:337
Letzte Seite:347
Fördernde Institution:Deutsche Forschungsgemeinschaft
Organisationseinheiten:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer Review:Referiert
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