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Abstract Fungal Δ9-fatty acid desaturases are self-sufficient enzymes in which the electron-donating cytochrome b5 (Cytb5) module is fused to the catalytic core, yet whether this covalent linkage is architecturally required has remained untested. Here we show that in the human pathogen Aspergillus fumigatus the Cytb5 module of the Δ9-desaturase SdeA must act in cis, within a self-associated complex organized by a hinge segment.
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