MaxEnt: −67.1% 5. Discussion. The first variant found in the two siblings was inherited from the healthy father and was on exon 4 (c.370 A>G), resulting in a missense mutation leading to the change of serine in position 124 to a glycine. The in silico analysis revealed a probable damaging effect of this variant: residue p.Ser124 indeed is highly conserved among species and seems to be located in the catalytic site of the enzyme, playing a pivotal role in NAD(H) binding to its substrate [20]. The first reaction during the conversion of steroid precursors is, in fact, the oxidation of the 3β-hydroxyl group to the ketone by the dehydrogenase activity, a process during which NAD+ is reduced to NADH. The intermediate Δ5,3-ketosteroid remains bound to the enzyme with nascent NADH, and the actual presence of NADH in the cofactor-binding site leads to the activation of the Δ5-Δ4-isomerase activity [5,7]. Due to the rarity of the disease, the phenotype–genotype correlation has not been fully investigated in a large case series. Albeit, in general, the functional and biochemical data are in agreement with the expressed phenotype, the clinical phenotype in the affected patients is significantly heterogeneous; moreover, identical DNA variants have been found in the HSD3B2 gene in patients showing a different clinical outcome [3,21,22].
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