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Mutations in the tetramer interface of human glucose‐6‐phosphate dehydrogenase reveals kinetic differences between oligomeric states
Author(s) -
Ranzani Americo Tavares,
Cordeiro Artur Torres
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12638
Subject(s) - tetramer , dimer , glucose 6 phosphate dehydrogenase , chemistry , dehydrogenase , enzyme , mutant , stereochemistry , biochemistry , crystallography , organic chemistry , gene
Glucose‐6‐phosphate dehydrogenase (G6PDH) catalyzes the oxidation of glucose‐6‐phoshate to 6‐phospho‐gluconolactone with the concomitant reduction of NADP + to NADPH . In solution, the recombinant human G6 PDH is known to be active as dimers and tetramers. To distinguish between the kinetic properties of dimers and tetramers of the G6 PDH is not trivial. Steady‐state kinetic experiments are often performed at low enzyme concentrations, which favor the dimeric state. The present work describes two novel human G6 PDH mutants, one that creates four disulfide bonds among apposing dimers, resulting in a ‘cross‐linked’ tetramer, and another that prevents the dimer to dimer association. The functional and structural characterizations of such mutants indicate the tetramer as the most active form of human G6 PDH .