HUMAN GLUCOSE-6-PHOSPHATE-DEHYDROGENASE - STRUCTURE AND FUNCTION OF NORMAL AND VARIANT ENZYMES

Glucose-6-phosphate dehydrogenase (G6PD) is a unique enzyme with many genetic variants. Recent progress in molecular biological techniques h ave provided several important findings about the structure-function r elationship of human G6PD. A putative substrate glucose-6-phosphate bi nding (around Lys 205) and a putative 'structural' NADP binding site ( around Lys 386) have been identified. A conservative segment (amino ac id 38-44) near the N-terminus was proposed to be the possible second N ADP binding region (amino acid 38-44). Analysis of amino acid substitu tions of variants revealed that there might be some relationship betwe en the position of substitution and the properties of variants.