Disease relevance of mog

• MogA was incapable of activating sulfite oxidase expressed in E. coli mogA(-) [1].
• The overlapping yaaG and yaaF genes from Bacillus subtilis were cloned and overexpressed in Escherichia coli [2].

High impact information on mog

• Here we show that moeA(-) and mogA(-) cells are able to synthesize molybdopterin, but both are deficient in molybdenum incorporation and, as a consequence, are deficient in the formation of molybdopterin-guanine dinucleotide [1].
• Purification of the gene products showed that yaaG encoded a homodimeric deoxyguanosine kinase (dGK) and that yaaF encoded a homodimeric deoxynucleoside kinase capable of phosphorylating both deoxyadenosine and deoxycytidine [2].
• The Aspergillus nidulans cnxABC locus is a single gene encoding two catalytic domains required for synthesis of precursor Z, an intermediate in molybdenum cofactor biosynthesis [3].
• In Escherichia coli, the MoaD protein plays a central role in the conversion of precursor Z to molybdopterin (MPT) during molybdenum cofactor biosynthesis [4].
• Mutations at the chlA or chlE locus, which are required for molybdenum cofactor biosynthesis, similarly do not affect the activity of the heat-treated extract in the in vitro activation process [5].

Chemical compound and disease context of mog

• Nitrate reductase in Escherichia coli K-12: involvement of chlC, chlE, and chlG loci [6].

Biological context of mog

• Such insertions also resulted in a Chlr and Pho- phenotype when the plasmid was in a delta (dye- chlG -phoM) phoR strain, although complementation tests suggested that the phoM+ and chlG + genes were still intact [7].

Associations of mog with chemical compounds

• None of the other known pleiotropic chlorate resistance loci (chlD, chlG) are required for the expression of its activity [5].
• The biotin sulfoxide reductase deficiency of a chlG, mutant is partially reversed by the addition of 10 mM molybdate to the growth medium [8].

References