level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover. The mutation results in a 35% reduction in acetaldehyde channeling efficiency
the variant has a 20fold higher catalytic efficiency for butyraldehyde and pentaldehyde compared to the catalytic efficiency of the wild type toward its natural substrate acetaldehyde. The mutation results in a 35% reduction in acetaldehyde channeling efficiency
the mutation does not substantially alter aldehyde channeling efficiencies. The level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover
level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover
site-directed mutagenesis, the barrier into the dehydrogenase active site region has been virtually eliminated such that acetaldehyde is transported from one active site to the other in a downhill process
site-directed mutagenesis, the barrier into the dehydrogenase active site region has been virtually eliminated such that acetaldehyde is transported from one active site to the other in a downhill process
generation of enzyme overexpressing mutant strain 10-6C, which is a photosynthetic mutant impaired in CO2 assimilation because of a point mutation in the RBCL gene
generation of enzyme overexpressing mutant strain 10-6C, which is a photosynthetic mutant impaired in CO2 assimilation because of a point mutation in the RBCL gene
expression of a mutant enzyme (with a glycine to aspartic acid mutation in the NADH binding site of the ADH domain of AdhE) in Pyrococcus furiosus from which the native aldehyde oxidoreductase (AOR) gene is deleted results in a reduced ethanol production to the background level
expression of a mutant enzyme (with a glycine to aspartic acid mutation in the NADH binding site of the ADH domain of AdhE) in Pyrococcus furiosus from which the native aldehyde oxidoreductase (AOR) gene is deleted results in a reduced ethanol production to the background level