title: Human glucose-6-phosphate dehydrogenase: structure and function of normal and variant enzymes.
abstract: Glucose-6-phosphate dehydrogenase (G6PD) is a unique enzyme with many genetic variants. Recent progress in molecular biological techniques have provided several important findings about the structure-function relationship of human G6PD. A putative substrate glucose-6-phosphate binding (around Lys 205) and a putative 'structural' NADP binding site (around Lys 386) have been identified. A conservative segment (amino acid 38-44) near the N-terminus was proposed to be the possible second NADP binding region (amino acid 38-44). Analysis of amino acid substitutions of variants revealed that there might be some relationship between the position of substitution and the properties of variants.
authors.affiliation: Okinaka Memorial Institute for Medical Research, Tokyo, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Hirono
authors.forename: S
authors.initials: S
authors.lastname: Miwa
mesh_terms: D000595:Amino Acid Sequence; D005954:Glucosephosphate Dehydrogenase / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D005955:Glucosephosphate Dehydrogenase Deficiency / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D005954:Glucosephosphate Dehydrogenase