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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
Author(s) -
Amrani Laïla,
Primus Jann,
Glatigny Annie,
Arcangeli Loretta,
Scazzocchio Claudio,
Finnerty Victoria
Publication year - 2000
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2000.02119.x
Subject(s) - biology , molybdenum cofactor , biochemistry , xanthine dehydrogenase , gene , aspergillus nidulans , azotobacter vinelandii , drosophila melanogaster , lyase , genetics , complementation , enzyme , nitrogenase , biosynthesis , xanthine oxidase , mutant , bacteria , nitrogen fixation
The molybdopterin cofactor (MoCF) is required for the activity of a variety of oxidoreductases. The xanthine oxidase class of molybdoenzymes requires the MoCF to have a terminal, cyanolysable sulphur ligand. In the sulphite oxidase/nitrate reductase class, an oxygen is present in the same position. Mutations in both the ma‐l gene of Drosophila melanogaster and the hxB gene of Aspergillus nidulans result in loss of activities of all molybdoenzymes that necessitate a cyanolysable sulphur in the active centre. 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. Key similarities were found with NifS, the enzyme involved in the generation of the iron–sulphur centres in nitrogenase. These similarities suggest an analogous mechanism for the generation of the terminal molybdenum‐bound sulphur ligand. We have identified putative homologues of these genes in a variety of organisms, including humans. The human homologue is located in chromosome 18.q12.