Glucose-6-Phosphate Dehydrogenase: Update and Analysis of New Mutations around the World

• Main Authors: Saúl Gómez-Manzo, Jaime Marcial-Quino, America Vanoye-Carlo, Hugo Serrano-Posada, Daniel Ortega-Cuellar, Abigail González-Valdez, Rosa Angélica Castillo-Rodríguez, Beatriz Hernández-Ochoa, Edgar Sierra-Palacios, Eduardo Rodríguez-Bustamante, Roberto Arreguin-Espinosa
• Format: Article
• Language: English
• Published: MDPI AG 2016-12-01
• Series: International Journal of Molecular Sciences
• Subjects: glucose-6-phosphate dehydrogenase (G6PD) enzyme; mutations; bioinformatics tools; three-dimensional structure; clinical manifestations
• Online Access: http://www.mdpi.com/1422-0067/17/12/2069

Glucose-6-phosphate dehydrogenase (G6PD) is a key regulatory enzyme in the pentose phosphate pathway which produces nicotinamide adenine dinucleotide phosphate (NADPH) to maintain an adequate reducing environment in the cells and is especially important in red blood cells (RBC). Given its central role in the regulation of redox state, it is understandable that mutations in the gene encoding G6PD can cause deficiency of the protein activity leading to clinical manifestations such as neonatal jaundice and acute hemolytic anemia. Recently, an extensive review has been published about variants in the g6pd gene; recognizing 186 mutations. In this work, we review the state of the art in G6PD deficiency, describing 217 mutations in the g6pd gene; we also compile information about 31 new mutations, 16 that were not recognized and 15 more that have recently been reported. In order to get a better picture of the effects of new described mutations in g6pd gene, we locate the point mutations in the solved three-dimensional structure of the human G6PD protein. We found that class I mutations have the most deleterious effects on the structure and stability of the protein.