4.1.99.13: (6-4)DNA photolyase

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For detailed information about (6-4)DNA photolyase, go to the full flat file.

Reaction

Synonyms

(6-4) DNA photolyase, (6-4) photolyase, (6-4) PHR, (6-4) PL, (6-4) PP-specific PL, (6-4)-Phr, (6-4)photolyase, 6-4 DNA photolyase, 6-4 photolyase, 6-4CiPhr, 6-4PP-photolyase, animal (6-4) photolyase, At64, At64PHR, bacterial (6-4) photolyase, CmPHR1, Cry1, CryB, deoxyribodipyrimidine photolyase-related protein, Dm64, DNA photolyase, Ds64PHR, H64PRH, human (6-4) photolyase homologous protein, NF-10, OtCPF1, phr (6-4), PhrB, PL-(6-4), prokaryotic (6-4) photolyase, RSP_3077, TRIREDRAFT_77473, XELAEV_18035355mg, Xl64phr

ECTree

     4 Lyases

         4.1 Carbon-carbon lyases

             4.1.99 Other carbon-carbon lyases

                4.1.99.13 (6-4)DNA photolyase

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Results	in table
8	Activating Compound
165	AA Sequence
1	CAS Registry Number
28	Cloned(Commentary)
50	Cofactor
7	Crystallization (Commentary)
13	Disease/ Diagnostics
7	Expression
56	General Information
10	Metals/Ions
8	Molecular Weight [Da]
28	Natural Substrates/ Products (Substrates)
65	Organism
3	PDB ID
16	pH Optimum
5	pH Range
1	pI Value
72	Protein Variants
21	Purification (Commentary)
30	Reaction
63	Reference
30	Source Tissue
5	Specific Activity [micromol/min/mg]
4	Storage Stability
66	Substrates and Products (Substrate)
3	Subunits
108	Synonyms
1	Systematic Name
8	Temperature Optimum [°C]

Systematic Name

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Systematic Name on EC 4.1.99.13 - (6-4)DNA photolyase

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SYSTEMATIC NAME

IUBMB Comments

(6-4) photoproduct pyrimidine-lyase

A flavoprotein (FAD). The overall repair reaction consists of two distinct steps, one of which is light-independent and the other one light-dependent. In the initial light-independent step, a 6-iminium ion is thought to be generated via proton transfer induced by two histidines highly conserved among the (6-4) photolyases. This intermediate spontaneously rearranges to form an oxetane intermediate by intramolecular nucleophilic attack. In the subsequent light-driven reaction, one electron is believed to be transferred from the fully reduced FAD cofactor (FADH-) to the oxetane intermediate thus forming a neutral FADH radical and an anionic oxetane radical, which spontaneously fractures. The excess electron is then back-transferred to the flavin radical restoring the fully reduced flavin cofactor and a pair of pyrimidine bases [2].