Purification and characterization of pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus
JM Blamey, MWW Adams - Biochimica et Biophysica Acta (BBA)-Protein …, 1993 - Elsevier
Pyrococcus furiosus grows optimally at 100° C by carbohydrate fermentation. It is thought to
contain a novel tungsten-dependent, NAD (P)-independent glycolytic pathway in which one
of the oxidation steps is catalyzed by a tungsten-containing aldehyde ferredoxin
oxidoreductase. The enzyme that catalyzes the terminal oxidation step, pyruvate ferredoxin
oxidoreductase (POR), has now been purified. POR has a molecular mass of 100 kDa and is
comprised of three subunits (45, 31 and 24 kDa). It lacks tungsten but contains thiamine …
contain a novel tungsten-dependent, NAD (P)-independent glycolytic pathway in which one
of the oxidation steps is catalyzed by a tungsten-containing aldehyde ferredoxin
oxidoreductase. The enzyme that catalyzes the terminal oxidation step, pyruvate ferredoxin
oxidoreductase (POR), has now been purified. POR has a molecular mass of 100 kDa and is
comprised of three subunits (45, 31 and 24 kDa). It lacks tungsten but contains thiamine …
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