Structure and function of glucose-6-phosphate dehydrogenase-deficient variants in Chinese population
| Autor: | Wenhong Ye, Haiyuan Li, Shan Duan, Yongshu He, Guo-long Yu, Weiying Jiang, Peng Liu, Jing Wen, Qian Geng, En Si, Qiuhong Tian, Chuan-shu Du, Yongmei Zheng, Qin Zhang, Yibin Guo, Chun Liu, Chengrui Jiang, Xiaoqin Ren, Qun-di Lin, Yan Qi, Lu-ming Chen |
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| Rok vydání: | 2006 |
| Předmět: |
Male
China congenital hereditary and neonatal diseases and abnormalities Population Dehydrogenase Glucosephosphate Dehydrogenase Glycogen Storage Disease Type I Biology Arginine medicine.disease_cause Protein Structure Secondary Denaturing high performance liquid chromatography Structure-Activity Relationship chemistry.chemical_compound hemic and lymphatic diseases parasitic diseases Genetics medicine Humans Glucose-6-phosphate dehydrogenase Genetic Testing Site-directed mutagenesis education Genetics (clinical) chemistry.chemical_classification Mutation education.field_of_study Genetic Variation nutritional and metabolic diseases Molecular biology Amino acid Glucosephosphate Dehydrogenase Deficiency Enzyme Amino Acid Substitution chemistry Female NADP |
| Zdroj: | Human Genetics. 119:463-478 |
| ISSN: | 1432-1203 0340-6717 |
| DOI: | 10.1007/s00439-005-0126-5 |
| Popis: | A systematic study on the structure and function of Glucose-6-phosphate dehydrogenase (G6PD) variations was carried out in China. A total of 155,879 participants were screened for G6PD deficiency by the G6PD/6PGD ratio method and 6,683 cases have been found. The prevalence of G6PD deficiency ranged from 0 to 17.4%. With informed consent, 1,004 cases from 11 ethnic-based groups were subjected to molecular analysis. Our results showed the followings: (1) The G6PD variants are consistent across traditional ethnic boundaries, but vary in frequencies across ethnic-based groups in Chinese population, (2) The G6PD variants in Chinese population are different from those in African, European, and Indian populations, (3) A novel G6PD-deficiency mutation, 274C--T, has been found, and (4) Denaturing high performance liquid chromatography is of great advantage to detecting G6PD-deficient mutations for diagnosis and genetic counseling. Moreover, functional analysis of the human G6PD variants showed the following: (1) The charge property, polarity, pK-radical and side-chain radical of the substituting amino acid have an effect on G6PD activity, (2) The G6PDArg459 and Arg463 play important roles in anchoring NADP+ to the catalytic domain to maintain the enzymatic activity, and (3) The sequence from codon 459 to the carboxyl terminal is essential for the enzymatic function. |
| Databáze: | OpenAIRE |
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