EC Number |
Protein Variants |
Reference |
---|
1.1.1.6 | A15T/D16G/V17A/N19K/E23D/Q45E/S46E/T47M/V48L/E49R/F52L/K53A/V58A/V59A/Q70H/D74N/G78D/E81G/T82N/Q83K/G86T/I88V/G108N/R139S/L142M/N145R/K155Q/V256I/L260M |
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae) |
710980 |
1.1.1.6 | D121A |
D121 can potentially hinder the proper binding of substrate 1,3-butanediol due to steric hindrance |
710980 |
1.1.1.6 | D121N |
mutation lowers the activity of the enzyme with most all the tested substrates relative to the native enzyme |
762346 |
1.1.1.6 | D121N/F245S |
mutant acquires D-lactate dehydrogenase activiy, the alteration increases the capacity of the glycerol binding site and facilitated hydrogen bonding between the S245 gamma-O and the C1 carboxylate of pyruvate |
762346 |
1.1.1.6 | D123N |
mutation abolishes the oxidative activity. The carboxylate of D123 is the base needed for abstracting the proton to form the alkoxy intermediate that precedes the hydride transfer to the nicotinamide cofactor |
760880 |
1.1.1.6 | D16N/N19A/E23D/L28M/E30N/R31N/Q45E/S46E/V48L/E49R/F52L/K53T/D54G/V58S/G78V/I79V/T82K/A83S/I88V/G108N/R139S/L142M/N145R/K155Q/L211I/G248S/V256I/H268Y/D317E/P319L |
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae) |
710980 |
1.1.1.6 | F245S |
mutant acquires D-lactate dehydrogenase activiy, the alteration increases the capacity of the glycerol binding site and facilitated hydrogen bonding between the S245 gamma-O and the C1 carboxylate of pyruvate |
762346 |
1.1.1.6 | I154A |
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme |
-, 739941 |
1.1.1.6 | I154A/K157G |
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme |
739941 |
1.1.1.6 | I154A/K157N |
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme |
739941 |