1.17.1.9 CO2 + NADH - 1.17.1.9 CO2 + NADH the enzyme exhibits a dramatic preference for the CO2 reduction reaction over the oxidation reaction of formate 1.17.1.9 formate + NAD+ - 1.17.1.9 formate + NAD+ enzyme provides NADH for synthesis 1.17.1.9 formate + NAD+ induced by methanol and formate 1.17.1.9 formate + NAD+ when Pseudomonas oxalaticus is grown on formate as main carbon and energy source, formate dehydrogenase is the key enzyme that generates NADH and CO 1.17.1.9 formate + NAD+ last step of methanol oxidation system 1.17.1.9 formate + NAD+ one of the key enzymes in the assimilation of C1 compounds, such as methanol 1.17.1.9 formate + NAD+ last enzyme of the dissimilatory pathway of the methanol metabolism 1.17.1.9 formate + NAD+ the level of formate dehydrogenase is considerably diminished without molybdenum, and in the presence of tungsten the activity was not detected in significant amounts 1.17.1.9 formate + NAD+ any one of the three formate dehydrogenases Fdh1, Fdh2 or Fdh3 is sufficient to sustain growth on formate. None is required for growth on methanol or methylamine 1.17.1.9 formate + NAD+ role of formate dehydrogenase in detoxification of exogenous formate 1.17.1.9 formate + NAD+ the enzyme shows strict substrate specificity for formate 1.17.1.9 formate + NAD+ the enzyme exhibits a dramatic preference for the CO2 reduction reaction over the oxidation reaction of formate 1.17.1.9 formate + NADP+ - 1.17.1.9 formate + NADP+ NADP+ is substrate for several mutant enzymes 1.17.1.9 formate + NADP+ NADP+ is a substrate for mutant enzymes only 1.17.1.9 additional information S-formylglutathione rather than free formate is an intermediate in oxidation of methanol by yeast 1.17.1.9 additional information possible role of enzyme in oxalate metabolism 1.17.1.9 additional information the enzyme shows no activity when methanol, ethanol, formaldehyde, sodium acetate, sodium malate, sodium oxalate, sodium lactate, sodium succinate, sodium citrate and sodium nitrate are used as the sole substrate 1.17.1.9 additional information the wild type enzyme shows no activity with NADP+