Literature summary extracted from
Henry, A.A.; Jimenez, R.; Hanway, D.; Romesberg, F.E.
Preliminary characterization of light harvesting in E. coli DNA photolyase (2004), ChemBioChem, 5, 1088-1094.
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
4.1.99.3 |
E109D |
mutant enzyme is unable to bind the methenyltetrahydrofolate cofactor under any conditions examined |
Escherichia coli |
4.1.99.3 |
E109Q |
mutant enzyme is unable to bind the methenyltetrahydrofolate cofactor under any conditions examined |
Escherichia coli |
4.1.99.3 |
H44F |
binds and retains methenyltetrahydrofolate under normal reconstitution conditions |
Escherichia coli |
4.1.99.3 |
H44F |
mutant enzyme retains no methenyltetrahydrofolate upon purification |
Escherichia coli |
4.1.99.3 |
L375H |
binds methenyltetrahydrofolate more weakly than wild-type enzyme |
Escherichia coli |
4.1.99.3 |
N108L |
binds and retains methenyltetrahydrofolate under normal reconstitution conditions |
Escherichia coli |
4.1.99.3 |
N108L |
mutant enzyme retains no methenyltetrahydrofolate upon purification |
Escherichia coli |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.1.99.3 |
Escherichia coli |
- |
- |
- |
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
4.1.99.3 |
methenyltetrahydrofolate |
the enzyme utilizes the the antenna cofactor to harvest light energy for the repair of thymine dimers in DNA. For this purpose, the enzyme evolved to bind the cofactor and red-shift its absorption maximum by 25 nm |
Escherichia coli |
|