Disease relevance of mal

• Comparison of the sequences of the Aspergillus nidulans hxB and Drosophila melanogaster ma-l genes with nifS from Azotobacter vinelandii suggests a mechanism for the insertion of the terminal sulphur atom in the molybdopterin cofactor [1].

High impact information on mal

• Linkage analysis located the disease locus at the centromeric region of bovine chromosome 24, where a ma-l homologous, putative molybdopterin cofactor sulfurase gene (MCSU) has been physically mapped [2].
• Evidence for the identity of in vitro reconstituted xanthine dehydrogenase from ma-l mutants with wild type enzyme is presented [3].
• The ma-l and hxB genes encode highly similar proteins containing domains common to pyridoxal phosphate-dependent cysteine transulphurases, including the cofactor binding site and a conserved cysteine, which is the putative sulphur donor [1].
• Two mutations affecting the red eye pigments (drosopterins), bw and mal, do not substantially perturb brown pigment synthesis in any of the four organs [4].
• Evidence for a new type of complementation among the cin, lxd and ma-l loci in Drosophila melanogaster [5].

Biological context of mal

• These alleles were isolated by taking full advantage of the pleiotropic phenotype exhibited by all previously described mal alleles and represent at least three unique examples of mal function [6].
• The tissue distributions of these enzymes are clearly disparate despite close linkage of their structural loci and parallel dependence on the mal, lxd, and cin loci [7].
• Ovaries taken from larvae produced by this cross were transplanted into female larval hosts of y f mal genotype, that were then mated to v f mal males [8].
• An analysis has been made of the effects of dietary molybdenum on lxd, lxd-c, lxd-d, lao (low aldehyde oxidase), mal (maroon-like eye color), and pac (Pacific) wild-type flies [9].

Associations of mal with chemical compounds

• Extracts of mal flies show normal levels of sulfite oxidase, whereas lxd flies have only 5-10% of the activity of wild type, and in cin flies the enzyme is apparently absent [10].
• The control of aldehyde oxidase and xanthine dehydrogenase activities and CRM levels by the mal locus in Drosophila melanogaster [6].
• Furthermore, two- to three-fold increases in specific activity of both enzymes occurred in all strains, except mal, when cultured on 5 x 10(-2) M molybdenum [9].

Other interactions of mal

• The molybdoenzyme system of Drosophila melanogaster. I. Sulfite oxidase: identification and properties. Expression of the enzyme in maroon-like (mal), low-xanthine dehydrogenase (lxd), and cinnamon (cin) flies [10].

Analytical, diagnostic and therapeutic context of mal

• Quantitative immunoelectrophoresis of ma-l and wild type extracts suggests that the ma-l function must be post-translational [11].

References