EC Number   |
Protein Variants |
Reference |
|---|
   1.4.9.1 | alphaF55A |
1656fold increase in Km-value for methylamine compared to wild-type enzyme, 484fold increase in Km-value for ethylamine compared to wild-type enzyme, 36fold increase in Km-value for propylamine compared to wild-type enzyme, 3.6fold decrease in Km-value for butylamine compared to wild-type enzyme, 53.2fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 34.3fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 54.3fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme |
656086 |
| 1.4.9.1 | alphaF55A |
inactivation by the mechanism-based inhibitor cyclopropylamine is accompanied by the formation of a covalent cross-link between the alpha and beta subunits of the enzyme. No cross-linking is seen with mutant enzymes alphaF55A or alphaF55I mutant enzymes |
655553 |
| 1.4.9.1 | alphaF55A |
mutation decreases the affinity for binding of monovalent cations, Na+ or K+. 1656fold increase in Km-value for methylamine compared to wild-type enzyme, 484fold increase in Km-value for ethylamine compared to wild-type enzyme, 36fold increase in Km-value for propylamine compared to wild-type enzyme, 3.6fold decrease in Km-value for butylamine compared to wild-type enzyme, 53.2fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 34.3fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 54.3fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme |
654866 |
| 1.4.9.1 | alphaF55A |
mutation increases the rate of the electron transfer reaction from the fully reduced tryptophan tryptophylquinone tryptophan tryptophylquinone methylamine dehydrogenase to amicyanin. Little difference in the overal structure of alphaF55A in complex with its electron acceptors, amicyanin and cytochrome c-551i, relative to the native complex. There are significant changes in the solvent content of the active site and substrate channel |
654628 |
| 1.4.9.1 | alphaF55I |
1.2fold decrease in Km-value for methylamine compared to wild-type enzyme, 18.9fold increase in Km-value for ethylamine compared to wild-type enzyme, 5.6fold increase in Km-value for propylamine compared to wild-type enzyme, 4.2fold decrease in Km-value for butylamine compared to wild-type enzyme, 10fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 7.3fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 6.7fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzym. Ability to discriminate between amines of different chain length is abolished |
656086 |
| 1.4.9.1 | alphaF55I |
inactivation by the mechanism-based inhibitor cyclopropylamine is accompanied by the formation of a covalent cross-link between the alpha and beta subunits of the enzyme. No cross-linking is seen with mutant enzymes alphaF55A or alphaF55I mutant enzymes |
655553 |
| 1.4.9.1 | alphaF55I |
mutation has no effect on binding of monovalent cation. 1.2fold decrease in Km-value for methylamine compared to wild-type enzyme, 18.9fold increase in Km-value for ethylamine compared to wild-type enzyme, 5.6fold increase in Km-value for propylamine compared to wild-type enzyme, 4.2fold decrease in Km-value for butylamine compared to wild-type enzyme, 10fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 7.3fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 6.7fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme |
654866 |
| 1.4.9.1 | betaD32N |
preparation contains a major species with six disulfides but no oxygen incorporated into betaTrp57 and a minor species with both oxygens incorporated, which is active. 1000fold increase in KM-value for methylamine |
656282 |
| 1.4.9.1 | betaD76N |
mutant enzyme is completely inactive |
656282 |
| 1.4.9.1 | betaI107N |
27.8fold increase in Km-value for methylamine compared to wild-type enzyme, 44.2fold increase in Km-value for ethylamine compared to wild-type enzyme, 8.5fold decrease in Km-value for propylamine compared to wild-type enzyme, 124fold decrease in Km-value for butylamine compared to wild-type enzyme, 62.5fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 23.2fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 5.6fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme |
654866 |
