TY - JOUR
T1 - Glucose-6-phosphate dehydrogenase
T2 - Update and analysis of new mutations around the world
AU - Gómez-Manzo, Saúl
AU - Marcial-Quino, Jaime
AU - Vanoye-Carlo, America
AU - Serrano-Posada, Hugo
AU - Ortega-Cuellar, Daniel
AU - González-Valdez, Abigail
AU - Castillo-Rodríguez, Rosa Angélica
AU - Hernández-Ochoa, Beatriz
AU - Sierra-Palacios, Edgar
AU - Rodríguez-Bustamante, Eduardo
AU - Arreguin-Espinosa, Roberto
N1 - Publisher Copyright:
© 2016 by the authors; licensee MDPI, Basel, Switzerland.
PY - 2016/12/9
Y1 - 2016/12/9
N2 - 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.
AB - 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.
KW - Bioinformatics tools
KW - Clinical manifestations
KW - Glucose-6-phosphate dehydrogenase (G6PD) enzyme
KW - Mutations
KW - Three-dimensional structure
UR - http://www.scopus.com/inward/record.url?scp=85006141577&partnerID=8YFLogxK
U2 - 10.3390/ijms17122069
DO - 10.3390/ijms17122069
M3 - Artículo de revisión
C2 - 27941691
AN - SCOPUS:85006141577
SN - 1661-6596
VL - 17
JO - International Journal of Molecular Sciences
JF - International Journal of Molecular Sciences
IS - 12
M1 - 2069
ER -