A functional mobA gene for molybdopterin cytosine dinucleotide cofactor biosynthesis is required for activity and holoenzyme assembly of the heterotrimeric nicotine dehydrogenases of Arthrobacter nicotinovorans.
Two Arthrobacter nicotinovorans molybdenum enzymes hydroxylate the pyridine ring of nicotine. Molybdopterin cytosine dinucleotide (MCD) was determined to be a cofactor of these enzymes. A mobA gene responsible for the formation of MCD could be identified and its function shown to be required for assembly of the heterotrimeric molybdenum enzymes.
Sachelaru
Paula
P
Institute for Biochemistry and Molecular Biology, University of Freiburg, Hermann-Herder-Strasse 7, 79104 Freiburg, Germany.
Schiltz
Emile
E
Brandsch
Roderich
R
D001173:Arthrobacter / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000235:genetics*; D003597:Cytosine Nucleotides / Q000096:biosynthesis* / Q000235:genetics; D004268:DNA-Binding Proteins / Q000235:genetics*; D019281:Dimerization; D015964:Gene Expression Regulation, Bacterial; D020035:Holoenzymes / Q000378:metabolism*; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism*; D011622:Pterins; D015534:Trans-Activators / Q000235:genetics*
D001426:Bacterial Proteins; D003597:Cytosine Nucleotides; D004268:DNA-Binding Proteins; D020035:Holoenzymes; D011622:Pterins; D015534:Trans-Activators; C066895:molybdopterin cytosine dinucleotide; D000587:Oxidoreductases Acting on CH-NH Group Donors; C066274:nicotine dehydrogenase