Literature summary extracted from
Park, S.J.; Cho, Y.D.
Studies on the active site of the Arabidopsis thaliana S-adenosylmethionine decarboxylase: Lys81 residue involvement in catalytic activity (2000), J. Biochem. Mol. Biol., 33, 69-74.
No PubMed abstract available
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.1.1.50 |
- |
Arabidopsis thaliana |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
4.1.1.50 |
K81A |
6fold higher substrate specificity with lysine, higher pH-optimum |
Arabidopsis thaliana |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
4.1.1.50 |
Salicylaldehyde |
inactivation, substrate protects |
Arabidopsis thaliana |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.1.1.50 |
Arabidopsis thaliana |
Q96286 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.1.1.50 |
recombinant enzyme, expression in Escherichia coli |
Arabidopsis thaliana |
Renatured (Commentary)
EC Number |
Renatured (Comment) |
Organism |
---|
4.1.1.50 |
dialysis of salicylaldehyde inactivated enzyme restores |
Arabidopsis thaliana |
pH Range
EC Number |
pH Minimum |
pH Maximum |
Comment |
Organism |
---|
4.1.1.50 |
6.8 |
7.3 |
wild-type enzyme |
Arabidopsis thaliana |
4.1.1.50 |
7.2 |
7.8 |
K81A mutant |
Arabidopsis thaliana |