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Literature summary extracted from

  • Rousseau, B.J.G.; Shafei, S.; Migliore, A.; Stanley, R.J.; Beratan, D.N.
    Determinants of photolyases DNA repair mechanism in Mesophiles and Extremophiles (2018), J. Am. Chem. Soc., 140, 2853-2861.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.3 cyclobutadipyrimidine (in DNA) Synechococcus elongatus PCC 7942 = FACHB-805
-
 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA) Escherichia coli
-
 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA) Thermus thermophilus
-
 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA) Sulfurisphaera tokodaii
-
 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA) Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA) Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA) Synechococcus elongatus PCC 7942 = FACHB-805 ATCC 27144 / PCC 6301 / SAUG 1402/1
-
 2 pyrimidine residues (in DNA)
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.3 Escherichia coli P00914
-
-
4.1.99.3 Sulfurisphaera tokodaii F9VNB1 i.e. Sulfurisphaera tokodaii
-
4.1.99.3 Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7 F9VNB1 i.e. Sulfurisphaera tokodaii
-
4.1.99.3 Synechococcus elongatus PCC 7942 = FACHB-805 P05327 i.e. Synechocystis sp.
-
4.1.99.3 Synechococcus elongatus PCC 7942 = FACHB-805 ATCC 27144 / PCC 6301 / SAUG 1402/1 P05327 i.e. Synechocystis sp.
-
4.1.99.3 Thermus thermophilus P61497
-
-
4.1.99.3 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 P61497
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.3 cyclobutadipyrimidine (in DNA)
-
 Synechococcus elongatus PCC 7942 = FACHB-805 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA)
-
 Escherichia coli 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA)
-
 Thermus thermophilus 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA)
-
 Sulfurisphaera tokodaii 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA)
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA)
-
 Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 cyclobutadipyrimidine (in DNA)
-
 Synechococcus elongatus PCC 7942 = FACHB-805 ATCC 27144 / PCC 6301 / SAUG 1402/1 2 pyrimidine residues (in DNA)
-
 ?
4.1.99.3 additional information enzyme in complex with CPD moiety, molecular docking study Synechococcus elongatus PCC 7942 = FACHB-805 ?
-
 ?
4.1.99.3 additional information enzyme in complex with CPD moiety, molecular docking study Escherichia coli ?
-
 ?
4.1.99.3 additional information enzyme in complex with CPD moiety, molecular docking study Thermus thermophilus ?
-
 ?
4.1.99.3 additional information enzyme in complex with CPD moiety, molecular docking study Sulfurisphaera tokodaii ?
-
 ?
4.1.99.3 additional information enzyme in complex with CPD moiety, molecular docking study Thermus thermophilus HB8 / ATCC 27634 / DSM 579 ?
-
 ?
4.1.99.3 additional information enzyme in complex with CPD moiety, molecular docking study Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7 ?
-
 ?
4.1.99.3 additional information enzyme in complex with CPD moiety, molecular docking study Synechococcus elongatus PCC 7942 = FACHB-805 ATCC 27144 / PCC 6301 / SAUG 1402/1 ?
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.3 FAD
-
 Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.3 FAD
-
 Escherichia coli
4.1.99.3 FAD
-
 Thermus thermophilus
4.1.99.3 FAD
-
 Sulfurisphaera tokodaii

General Information

EC Number General Information Comment Organism
4.1.99.3 additional information enzyme structure comparisons and molecular modeling, overview. The enzyme AnPL from Anacystis nidulans is mesophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Sulfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping Synechococcus elongatus PCC 7942 = FACHB-805
4.1.99.3 additional information enzyme structure comparisons and molecular modeling, overview. The enzyme EcPL from Escherichia coli is mesophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Sulfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping Escherichia coli
4.1.99.3 additional information enzyme structure comparisons and molecular modeling, overview. The enzyme from Thermus thermophilus is thermophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Solfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping Thermus thermophilus
4.1.99.3 additional information enzyme structure comparisons and molecular modeling, overview. The enzyme from Sulfolobus tokodaii is hyperthermophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Solfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping Sulfurisphaera tokodaii