A rare G6PD variant (c.383T>G; p.128Leu>Arg) with a molecular pathophysiological mechanism similar to that of G6PD A- (68Val>Met, 126Asn>Asp).
We report the second documented observation of a rare class-III variant, we named G6PD Pyrgos, [c.383 T>G, p.128Leu>Arg] found in a Greek family. A 3-dimensional structure model for the enzyme shows that the region modified by the substitution is identical to that modified in G6PD A(-) (68Val>Met, 126Asn>Asp), suggesting a common underlying pathophysiological mechanism. Observation of this mutation in different Mediterranean regions suggests that it might be more widespread that initially supposed and, in the absence of molecular characterization, could be confused with other frequent variants.
Moradkhani
Kamran
K
INSERM, U955, Créteil, F-94010, France. Kamran.Moradkhani@inserm.fr
Bahuau
Michel
M
Préhu
Claude
C
Martin
Natacha
N
Bimet
Catherine
C
Galactéros
Frederic
F
Wajcman
Henri
H
D019943:Amino Acid Substitution / Q000235:genetics; D005091:Exons / Q000235:genetics; D005260:Female; D014644:Genetic Variation / Q000235:genetics; D005954:Glucosephosphate Dehydrogenase / Q000737:chemistry / Q000235:genetics*; D006115:Greece; D006801:Humans; D008297:Male; D009154:Mutation; D011487:Protein Conformation
D005954:Glucosephosphate Dehydrogenase; C482910:glucose-6-phosphate dehydrogenase A-