EC Number   |
Protein Variants |
Reference |
|---|
    1.1.3.13 | F101N |
with enlarged catalytic cavity, increase in activity with substrates 1-propanol, glycerol, (R)-1,2-propanediol |
762732 |
| 1.1.3.13 | F101S |
with enlarged catalytic cavity, retains a high degree of thermostability |
762732 |
| 1.1.3.13 | G15A |
mutastion in putative FAD-binding domain, prevents enzyme import into peroxisome and assembly |
656760 |
| 1.1.3.13 | M103S |
with enlarged catalytic cavity, increase in activity with substrates 1-propanol, glycerol, (R)-1,2-propanediol |
762732 |
| 1.1.3.13 | M359R |
mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13 |
762910 |
| 1.1.3.13 | more |
alcohol dehydrogenase is expressed with a thermostable NADPH-oxidase fusion partner (phenylacetone monooxygenase C65D) and purified. The resulting bifunctional biocatalyst retains the catalytic properties of the individual enzymes, and acts essentially like alcohol oxidase, while merely requiring a catalytic amount of NADP+ |
762911 |
| 1.1.3.13 | more |
analysis of the regulation of native alcohol oxidase expression in Pichia pastoris Mut+ strain expressing a recombinant avidin |
673395 |
| 1.1.3.13 | more |
construction of an inactive double-knockout mutant of FAO1 by gene deletion, the mutant is incapable to grow on octadecane, but grows well on oleic acid, palmitic acid, and shorter chain alkanes/fatty acids, overview, an additional spontenaous mutation of the double mutant leads to loss of the ability to grow on oleic acid and hexadecane |
672339 |
| 1.1.3.13 | more |
deletion of 1,4,10, or 16 C-terminal amino acids, normal import into peroxisome and assembly to octamer. Deletion of C-terminal 22 amino acids, growth of cells ceases at an OD corresponding to midexponential growth stage, more than 90% reduction of enzymic activity, enzyme is localized both to peroxisome and cytosol |
656760 |
| 1.1.3.13 | more |
enzyme immobilization on DEAE-cellulose particles for alcohol biosensor applications, substrate specificity and the optimum pH of the immobilized enzyme are similar to those of the free enzyme, while Km and temperature optimum differ, overview |
697064 |
