Disease relevance of moeA

• Physiological and genetic analyses leading to identification of a biochemical role for the moeA (molybdate metabolism) gene product in Escherichia coli [1].
• The narA locus of Synechococcus sp. strain PCC 7942 consists of a cluster of molybdopterin biosynthesis genes [2].
• Activity of the molybdopterin-containing xanthine dehydrogenase of Rhodobacter capsulatus can be restored by high molybdenum concentrations in a moeA mutant defective in molybdenum cofactor biosynthesis [3].

High impact information on moeA

• Wild-type (chl+) cells are inhibited by addition of 200 microM nitrate, but chlA, chlB, and chlE mutants are not [4].
• These results indicate that although a guanosine compound serves as the initial precursor for molybdopterin biosynthesis, the early steps of this pathway in E. coli proceed via a pathway unlike that of any known pteridine biosynthetic pathway [5].
• The expression of the moa locus, which encodes enzymes required for molybdopterin biosynthesis, is enhanced under anaerobiosis but repressed when the bacterium is able to synthesize active molybdenum cofactor [6].
• Synechococcus mutants bearing only inactive versions of this putative moeB gene could not be isolated suggesting that it has function(s) additional to molybdopterin biosynthesis [7].
• Interposon mutants defective in moeA did not exhibit dimethyl sulfoxide reductase or nitrate reductase activity, which both require the molybdopterin guanine dinucleotide (MGD) cofactor, even after addition of 1 mM molybdate to the medium [3].

Chemical compound and disease context of moeA

• Nitrate reductase in Escherichia coli K-12: involvement of chlC, chlE, and chlG loci [8].

Biological context of moeA

• Addition of sulfide to the growth medium of moeA cys double mutants suppressed the MoeA- phenotype [1].
• Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis [9].

Anatomical context of moeA

• The nitrate reductase in the wild type was completely stable in vivo under inducing or noninducing conditions, whereas in the chlC and chlE mutants nitrate reductase was degraded extensively in both the cytoplasm and membranes, even under inducing conditions [10].

Associations of moeA with chemical compounds

• Heat-treated preparations from chlA and chlE mutants which do not possess molybdenum cofactor activity fail to restore the activation [11].

Other interactions of moeA

• Involvement of chlA, E, M, and N loci in Escherichia coli molybdopterin biosynthesis [12].

Analytical, diagnostic and therapeutic context of moeA

• E. coli JRG97 cells transformed with mutants that failed to restore nitrate reductase activity showed by HPLC analysis a decreased level of molybdopterin-derived dephospho FormA as compared to bacteria transformed with wild-type moeA [13].

References