TY  - JOUR
A1  - Mendel, Ralf R.
A1  - Leimkühler, Silke
T1  - The biosynthesis of the molybdenum cofactors
T2  - Journal of biological inorganic chemistry
N2  - 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.
KW  - Molybdenum
KW  - Molybdenum cofactor
KW  - cPMP
KW  - bis-MGD
KW  - Sulfuration
KW  - Sulfite oxidase
Y1  - 2015
UR  - https://publishup.uni-potsdam.de/frontdoor/index/index/docId/39127
SN  - 0949-8257
SN  - 1432-1327
VL  - 20
IS  - 2
SP  - 337
EP  - 347
PB  - Springer
CY  - New York
ER  -