1.5.3.16: spermine oxidase
This is an abbreviated version!
For detailed information about spermine oxidase, go to the full flat file.
Word Map on EC 1.5.3.16
-
1.5.3.16
-
polyamine
-
putrescine
-
acetylpolyamine
-
back-conversion
-
n1-acetylspermine
-
n1-acetylpolyamine
-
3-aminopropanal
-
acrolein
-
benspm
-
medicine
- 1.5.3.16
- polyamine
- putrescine
-
acetylpolyamine
-
back-conversion
- n1-acetylspermine
-
n1-acetylpolyamine
- 3-aminopropanal
- acrolein
-
benspm
- medicine
Reaction
Synonyms
AtPAO1, AtPAO4, AtPAO5, EC 1.5.3.11, Fms1 protein, GhPAO, hSMO, MmSMO, mSMO, mSMOalpha, mSMOmu, PAO, PAO1, PAO4, PAO5, PAO6, PAO7, PAOh1, PAOh1/SMO, SelPAO5, SMO, SMO(PAOh1), SMO/PAOh1, SMO5, SMOX, spermine oxidase, Spm oxidase, thermospermine oxidase
ECTree
Advanced search results
Engineering
Engineering on EC 1.5.3.16 - spermine oxidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
E216L/S218A
mutation E216L/S218A endows the enzyme with N1-acetylspermine oxidase activity
H82E
H82Q
K367M
additional information
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
construction of a knock-out mutant that has a T-DNA insertion within the ninth exon of the AtPAO4 gene, and of a knock-down mutant Atpao4i with reduced expression by RNAi under control of the CMV 35S promoter. AtPAO4 deficiency induces alterations in the expression of genes related to the drought stress response and flavonoid biosynthesis
additional information
purified mutant mSMOmuDELTA (with a deletion of the nuclear domain A) exhibits biochemical properties very similar to that of mSMOalpha and mSMOmu, in particular a pH optimum of 8.5 in 0.1 m Na-phosphate buffer, a Km value of 0.222 mM and a kcat value of 0.0208 per sec. Removal of the nuclear domain amino acid region abolishes proper nuclear targeting of the mSMOmu isoform
additional information
-
purified mutant mSMOmuDELTA (with a deletion of the nuclear domain A) exhibits biochemical properties very similar to that of mSMOalpha and mSMOmu, in particular a pH optimum of 8.5 in 0.1 m Na-phosphate buffer, a Km value of 0.222 mM and a kcat value of 0.0208 per sec. Removal of the nuclear domain amino acid region abolishes proper nuclear targeting of the mSMOmu isoform
additional information
-
wild-type and mutant proteins share essentially the same structural properties. The pH-dependency of the catalytic activity of H82Q is essentially unchanged with respect to the wild-type, while a slight shift toward higher pH values is observed for the K367M mutant
additional information
wild-type and mutant proteins share essentially the same structural properties. The pH-dependency of the catalytic activity of H82Q is essentially unchanged with respect to the wild-type, while a slight shift toward higher pH values is observed for the K367M mutant
additional information
a mutant enzyme deprived of all but two cysteine residues (C263/C429) results in a monomeric enzyme species. The mutant enzyme is less stable than the wild type. Is activity decreased by about 90% after 1 day from the preparation, and storage at 6°C or -20°C