caa a22 4500 605507813 CHVBK 20210128100633.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00775-014-1173-y doi (NATIONALLICENCE)springer-10.1007/s00775-014-1173-y The biosynthesis of the molybdenum cofactors [Elektronische Daten] [Ralf Mendel, Silke Leimkühler] 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) 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. SBIC, 2014 Molybdenum nationallicence Molybdenum cofactor nationallicence cPMP nationallicence bis-MGD nationallicence Sulfuration nationallicence Sulfite oxidase nationallicence Mendel Ralf Institute of Plant Biology, Braunschweig University of Technology, Humboldtstr. 1, 38106, Braunschweig, Germany aut Leimkühler Silke Department of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476, Potsdam, Germany aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 337-347 0949-8257 20:2<337 2015 20 775 https://doi.org/10.1007/s00775-014-1173-y text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-014-1173-y text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Mendel Ralf Institute of Plant Biology, Braunschweig University of Technology, Humboldtstr. 1, 38106, Braunschweig, Germany aut NATIONALLICENCE 700 1- Leimkühler Silke Department of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476, Potsdam, Germany aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 337-347 0949-8257 20:2<337 2015 20 775