EC Number   |
Protein Variants |
Reference |
|---|
   1.5.3.14 | E170Q |
mutation results in moderate change of enzyme activity and apparent Km-values |
672006 |
| 1.5.3.14 | E62Q |
mutation results in moderate change of enzyme activity and apparent Km-values |
672006 |
| 1.5.3.14 | K300M |
mutation results in a 1400fold decrease in the rate of flavin reduction and a 160fold decrease in the equilibrium dissociation constant for the K300M-spermidine complex, consistent with a major role for this residue in the mechanism of substrate oxidation |
672006 |
| 1.5.3.14 | K300M |
site-directed mutagenesis, catalyitically impaired active site mutant, that is less glycosylated than the wild-type enzyme. The mutant shows a 1400fold decrease in the rate of flavin reduction. Substrates are bound in an out-of-register mode and the HOH309 water molecule is absent in the enzymesubstrate complexes. K300 mutation brings about a 60 mV decrease in the FAD redox potential and a 30fold decrease in the FAD reoxidation rate, within a virtually unaltered geometry of the catalytic pocket |
724968 |
| 1.5.3.14 | more |
transgenic Mpao overexpressing tobacco plants show highly increased enzyme activity and 1,3-diaminopropane levels, also specific isoforms of the antioxidant machinery, i.e. peroxidase, superoxide dismutase and catalase, are induced in the transgenics but not in the wild-type, along with increase in activities of additional enzymes contributing to redox homeostasis. Nevertheless, further increase in the intracellular reactive oxygen species by exogenous H2O2, or addition of methylviologen or menadione to transgenic leaf discs, results in oxidative stress as evidenced by the lower quantum yield of PSII, the higher ion leakage, lipid peroxidation and induction of programmed cell death, overview |
694583 |
| 1.5.3.14 | Y298F |
specific activity or KM-values are not substantially altered |
672006 |
