Source: http://ezcatdb.cbrc.jp/EzCatDB/search/get.do?dbcode=S00016
Timestamp: 2019-04-26 09:42:50+00:00

Document:
Endonucleolytic cleavage near pyrimidine dimers to products with 5''-phosphate.
Preliminary crystallographic study of pyrimidine dimer-specific excision-repair enzyme from bacteriophage T4.
Structure-function studies of the T4 endonuclease V repair enzyme.
Site-directed mutagenesis of the T4 endonuclease V gene: mutations which enhance enzyme specific activity at low salt concentrations.
Mutations in endonuclease V that affect both protein-protein association and target site location.
Selective metal binding to Cys-78 within endonuclease V causes an inhibition of catalytic activities without altering nontarget and target DNA binding.
Reductive methylation of the amino terminus of endonuclease V eradicates catalytic activities. Evidence for an essential role of the amino terminus in the chemical mechanisms of catalysis.
Site-directed deletion mutagenesis within the T4 endonuclease V gene: dispensable sequences within putative loop regions.
Atomic structure of a pyrimidine-dimer specific excision-repair enzyme from bacteriophage T4.
Participation of glutamic acid 23 of T4 endonuclease V in the beta-elimination reaction of an abasic site in a synthetic duplex DNA.
Role of the basic amino acid cluster and Glu-23 in pyrimidine dimer glycosylase activity of T4 endonuclease V.
X-ray structure of T4 endonuclease V: an excision repair enzyme specific for a pyrimidine dimer.
Structure/function analysis of the Ala116-->Lys121 region of endonuclease V by random targeted mutagenesis.
T4 endonuclease V. Perspectives on catalysis.
Crystal structure of T4 endonuclease V. An excision repair enzyme for a pyrimidine dimer.
Nuclear magnetic resonance study of the interaction of T4 endonuclease V with DNA.
Reaction mechanism of T4 endonuclease V determined by analysis using modified oligonucleotide duplexes.
Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNA substrate: structural basis for damaged DNA recognition.
Involvement of glutamic acid 23 in the catalytic mechanism of T4 endonuclease V.
Crystal structure of a pyrimidine dimer-specific excision repair enzyme from bacteriophage T4: refinement at 1.45 A and X-ray analysis of the three active site mutants.
Structural determinants for specific recognition by T4 endonuclease V.
Role of specific amino acid residues in T4 endonuclease V that alter nontarget DNA binding.
The role of base flipping in damage recognition and catalysis by T4 endonuclease V.
Characterization of a novel cis-syn and trans-syn-II pyrimidine dimer glycosylase/AP lyase from a eukaryotic algal virus, Paramecium bursaria chlorella virus-1.
Three-dimensional structural views of damaged-DNA recognition: T4 endonuclease V, E. coli Vsr protein, and human nucleotide excision repair factor XPA.
Processivity of DNA repair enzymes.
Interaction of T4 endonuclease V with DNA: importance of the flexible loop regions in protein-DNA interaction.
Although this enzyme classified into hydrolase (E.C. 3.-.-.-), it does not catalyzes hydrolysis. According to the literature , , ,  & , this enzyme catalyzes the following reactions succesively, although the detailed mechanism has not been elucidated.
(I) glycosylase reaction to form Schiff-base intermediate.
(A) Transfer of deoxyribose group from pyrimidine dimer to the N-terminal alpha-amino group.
(B) Eliminative double-bond formation; Ring opening of deoxyribose, forming Schiff-base intermediate.
(C) Isomerization; Shift of double-bond from Schiff-base to adjacent bond.
(D) Eliminative double-bond formation; beta-elimination of 3'-phosphate from the opened deoxyribose group.
The N-terminal alpha-amino group of Thr2 forms Schiff-base with C1' atom of the deoxyribose. Glu23 seems to be required for both reactions, (I) & (II).

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