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Literature summary for 4.1.99.3 extracted from
- Electron transfer pathways of cyclobutane pyrimidine dimer photolyase revisited (2018), J. Phys. Chem. B, 122, 6912-6921 .
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cyclobutadipyrimidine (in DNA) | Synechococcus elongatus PCC 7942 = FACHB-805 | - |
2 pyrimidine residues (in DNA) | - |
? |  |
| cyclobutadipyrimidine (in DNA) | Synechococcus elongatus PCC 7942 = FACHB-805 ATCC 27144 / PCC 6301 / SAUG 1402/1 | - |
2 pyrimidine residues (in DNA) | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Synechococcus elongatus PCC 7942 = FACHB-805 | P05327 | i.e. Synechocystis sp. | - |
| Synechococcus elongatus PCC 7942 = FACHB-805 ATCC 27144 / PCC 6301 / SAUG 1402/1 | P05327 | i.e. Synechocystis sp. | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) | molecular mechanism of the electron transfer, overview. The electronic coupling matrix element is 36/cm from the donor (FADH-) to the acceptor (CPD) by Mulliken-Hush (GMH) method and the bridge green function (GF) methods, and the estimated electron transfer time is 386 ps. Molecular dynamics simulations and ab initio molecular orbital calculations, and exploration of the electron tunneling pathway for 20 different structures during the MD trajectory, QM/MM calculation. The electron transfer route via Asn349 is the dominant pathway among the five major routes via (adenine/Asn349), (adenine/Glu283), (adenine/Glu283/Asn349/Met353), (Met353/Asn349), and (Asn349), indicating that Asn349 is an essential amino acid residue in the electron transfer reaction | Synechococcus elongatus PCC 7942 = FACHB-805 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cyclobutadipyrimidine (in DNA) | - |
Synechococcus elongatus PCC 7942 = FACHB-805 | 2 pyrimidine residues (in DNA) | - |
? | |
| cyclobutadipyrimidine (in DNA) | - |
Synechococcus elongatus PCC 7942 = FACHB-805 ATCC 27144 / PCC 6301 / SAUG 1402/1 | 2 pyrimidine residues (in DNA) | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CPD photolyase | - |
Synechococcus elongatus PCC 7942 = FACHB-805 |
| cyclobutane pyrimidine dimer photolyase | - |
Synechococcus elongatus PCC 7942 = FACHB-805 |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | the adenine moiety of FADH- bridges between the electron donating isoalloxazine ring and CPD via two hydrogen bonds, suggesting the presence of electron transfer pathways via adenine | Synechococcus elongatus PCC 7942 = FACHB-805 | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | to analyze the UV-induced DNA lesion repair mechanism, the excited states of the active site (including the electron donor and acceptor) is calculated | Synechococcus elongatus PCC 7942 = FACHB-805 |
| physiological function | the photoinduced electron transfer (ET) reaction of cyclobutane pyrimidine dimer (CPD) photolyase plays an essential role in its DNA repair reaction | Synechococcus elongatus PCC 7942 = FACHB-805 |
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