The Role of the Nucleotides in the Insertion of the bis-Molybdopterin Guanine Dinucleotide Cofactor into apo-Molybdoenzymes

The role of the GMP nucleotides of the bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor of the DMSO reductase family has long been a subject of discussion. The recent characterization of the bis-molybdopterin (bis-Mo-MPT) cofactor present in the E. coli YdhV protein, which differs from bis-...

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Bibliographic Details
Published inMolecules (Basel, Switzerland) Vol. 27; no. 9; p. 2993
Main Authors Tiedemann, Kim, Iobbi-Nivol, Chantal, Leimkühler, Silke
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 06.05.2022
MDPI
Subjects
Bacteria
Binding sites
Biosynthesis
bis-MGD
chaperone
Dehydrogenases
E coli
Enzymes
Life Sciences
Molybdenum
molybdenum cofactor
Nitrates
Organisms
Phosphate esters
Prokaryotes
Proteins
TMAO reductase
bis-MGD
chaperone
molybdenum cofactor
TMAO reductase
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Summary:The role of the GMP nucleotides of the bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor of the DMSO reductase family has long been a subject of discussion. The recent characterization of the bis-molybdopterin (bis-Mo-MPT) cofactor present in the E. coli YdhV protein, which differs from bis-MGD solely by the absence of the nucleotides, now enables studying the role of the nucleotides of bis-MGD and bis-MPT cofactors in Moco insertion and the activity of molybdoenzymes in direct comparison. Using the well-known E. coli TMAO reductase TorA as a model enzyme for cofactor insertion, we were able to show that the GMP nucleotides of bis-MGD are crucial for the insertion of the bis-MGD cofactor into apo-TorA.
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ISSN:1420-3049
1420-3049
DOI:10.3390/molecules27092993