High impact information on cin

• Altogether 59 cistrons have been identified, including five ellelic with previously known loci: cin, fs(1)N, mk, sn, and r [1].
• The low molecular weight molybdenum cofactor is found to be severely reduced in extracts of the 1xd and cin mutants but ma--1 mutants have high levels of cofactor [2].
• Evidence for a new type of complementation among the cin, lxd and ma-l loci in Drosophila melanogaster [3].
• All cin allelic heterozygotes, which were defined as complementing in adults, less then 24h of age, displayed similar levels of complementation at all stages tested [4].
• The developmental analysis of aldehyde oxidase activity in cin allelic heterozygotes of Drosophila melanogaster [4].

Biological context of cin

• 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 [5].

Associations of cin 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 [6].

Other interactions of cin

• 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 [6].
• The other AO-deficient mutants that were examined are cin, mal, and lxd; each has appreciable levels of CRM in both larval hemolymph and adult extract [7].

References