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Literature summary extracted from

  • Sancar, A.
    Structure and function of photolyase and in vivo enzymology: 50th Anniversary (2008), J. Biol. Chem., 283, 32153-32157.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.3 additional information Escherichia coli absolute dependence of catalysis by photolyase on light ?
-
?
4.1.99.3 additional information Streptomyces griseus absolute dependence of catalysis by photolyase on light ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.3 Escherichia coli
-
-
-
4.1.99.3 no acitivity in Haemophilus influenzae
-
-
-
4.1.99.3 Streptomyces griseus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.3 cyclobutadipyrimidine in DNA
-
Escherichia coli pyrimidine residues in DNA
-
?
4.1.99.3 cyclobutadipyrimidine in DNA
-
Streptomyces griseus pyrimidine residues in DNA
-
?
4.1.99.3 additional information absolute dependence of catalysis by photolyase on light Escherichia coli ?
-
?
4.1.99.3 additional information absolute dependence of catalysis by photolyase on light Streptomyces griseus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
4.1.99.3 CPD photolyase
-
Escherichia coli
4.1.99.3 CPD photolyase
-
Streptomyces griseus
4.1.99.3 photolyase
-
Escherichia coli
4.1.99.3 photolyase
-
Streptomyces griseus
4.1.99.3 photoreactivating enzyme
-
Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.3 5,10-methenyltetrahydrofolate
-
Escherichia coli
4.1.99.3 5,10-methenyltetrahydrofolate
-
Streptomyces griseus
4.1.99.3 FAD the photolyase in its native state contains FAD in the two-electron reduced and deprotonated FADH- form, during purification under aerobic conditions, FADH- is oxidized to the rather stable blue neutral radical Escherichia coli
4.1.99.3 FAD the photolyase in its native state contains FAD in the two-electron reduced and deprotonated FADH- form, during purification under aerobic conditions, FADH- is oxidized to the rather stable blue neutral radical Streptomyces griseus