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The biosynthesis of the molybdenum cofactors in Escherichia coli
Author(s) -
Leimkühler Silke
Publication year - 2020
Publication title -
environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.954
H-Index - 188
eISSN - 1462-2920
pISSN - 1462-2912
DOI - 10.1111/1462-2920.15003
Subject(s) - molybdenum cofactor , pterin , biosynthesis , escherichia coli , cofactor , biochemistry , nucleotide , molybdenum , biology , sulfur , gtp' , stereochemistry , chemistry , enzyme , gene , organic chemistry
Summary The biosynthesis of the molybdenum cofactor (Moco) is highly conserved among all kingdoms of life. In all molybdoenzymes containing Moco, the molybdenum atom is coordinated to a dithiolene group present in the pterin‐based 6‐alkyl side chain of molybdopterin (MPT). In general, the biosynthesis of Moco can be divided into four steps in in bacteria: (i) the starting point is the formation of the cyclic pyranopterin monophosphate (cPMP) from 5′‐GTP, (ii) in the second step the two sulfur atoms are inserted into cPMP leading to the formation of MPT, (iii) in the third step the molybdenum atom is inserted into MPT to form Moco and (iv) in the fourth step bis‐Mo‐MPT is formed and an additional modification of Moco is possible with the attachment of a nucleotide (CMP or GMP) to the phosphate group of MPT, forming the dinucleotide variants of Moco. This review presents an update on the well‐characterized Moco biosynthesis in the model organism Escherichia coli including novel discoveries from the recent years.