Literature summary for 4.1.99.3 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.

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Protein Variants

Protein Variants	Comment	Organism
E109D	mutant enzyme is unable to bind the methenyltetrahydrofolate cofactor under any conditions examined	Escherichia coli
E109Q	mutant enzyme is unable to bind the methenyltetrahydrofolate cofactor under any conditions examined	Escherichia coli
H44F	binds and retains methenyltetrahydrofolate under normal reconstitution conditions	Escherichia coli
H44F	mutant enzyme retains no methenyltetrahydrofolate upon purification	Escherichia coli
L375H	binds methenyltetrahydrofolate more weakly than wild-type enzyme	Escherichia coli
N108L	binds and retains methenyltetrahydrofolate under normal reconstitution conditions	Escherichia coli
N108L	mutant enzyme retains no methenyltetrahydrofolate upon purification	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Cofactor

Cofactor	Comment	Organism	Structure
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

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Release 2023.1 (January 2023)