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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 by Laïla Amrani; Jann Primus; Annie Glatigny; Loretta Arcangeli; Claudio Scazzocchio; Victoria Finnerty is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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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.

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Author

Laïla Amrani; Jann Primus; Annie Glatigny; Loretta Arcangeli; Claudio Scazzocchio; Victoria Finnerty

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0950-382X)

Published

2000

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)