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4.2.99.18: DNA-(apurinic or apyrimidinic site) lyase

This is an abbreviated version!
For detailed information about DNA-(apurinic or apyrimidinic site) lyase, go to the full flat file.

Word Map on EC 4.2.99.18

Reaction

the C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate =

Synonyms

8-oxoG DNA glycosylase, abasic (AP)-endonuclease, abasic endonuclease, AdAPE1/Ref-1, Af0371, Afogg enzyme, ALKBH1, AP 1, AP DNA endonuclease 1, AP Dnase, AP endo, AP endonuclease, AP endonuclease 1, AP endonuclease Ape1, AP endonuclease Class I, AP endonuclease I, AP endonuclease VI, AP lyase, AP site-DNA 5'-phosphomonoester-lyase, AP-endonuclease, AP-endonuclease 1, AP-endonuclease 2, AP-endonuclease/3'-5'exodeoxyribonuclease, AP-lyase, Ap1, Ap2, Ape, APE-1, APE/Ref-1, APE1, APE1/Ref-1, Ape1L, Ape2, APEN, APEX nuclease, APEX1, APLM, APN, APN-1, APN1, apurinic DNA endonuclease, apurinic endodeoxyribonuclease, apurinic endonuclease, apurinic endonuclease 1, apurinic-apyrimidinic DNA endonuclease, apurinic-apyrimidinic endodeoxyribonuclease, apurinic-apyrimidinic endonuclease, apurinic-apyrimidinic endonuclease 1, apurinic-apyrimidinic endonuclease I, apurinic/apyrimidic endonuclease 1, apurinic/Apyrimidinic (AP) endonuclease 1, apurinic/apyrimidinic AP endonuclease, apurinic/apyrimidinic DNA endonuclease 1, apurinic/apyrimidinic endonuclease, apurinic/apyrimidinic endonuclease 1, apurinic/apyrimidinic endonuclease 1/redox factor-1, apurinic/apyrimidinic endonuclease 2, apurinic/apyrimidinic endonuclease APE1, apurinic/apyrimidinic endonuclease-1, apurinic/apyrimidinic endonuclease-1/Redox factor-1, apurinic/apyrimidinic endonuclease/redox effector factor-1, Apurinic/apyrimidinic endonuclease1/redox factor 1, apurinic/apyrimidinic endonuclease1/redox factor-1, apurinic/apyrimidinic lyase, apurinic/apyrimidinic site lyase, apurinic/apyrimidinic specific endonuclease, apurinic/apyrimidinic-endonuclease, apyrimidinic endonuclease, archaeal GO glycosylase, BAP1, class II AP endonuclease LMAP, class II apurinic/apyrimidinic(AP)-endonuclease, class-II AP-endonuclease, deoxyribonuclease (apurinic or apyrimidinic), DNA lyase, DNA polymerase X, DNA-(apurinic or apyrimidinic site) lyase, E. coli endonuclease III, EC 3.1.25.2, EcoNth, Endo III, endodeoxyribonuclease, endodeoxyribonuclease III, EndoIV, endonuclease III, endonuclease IV, endonuclease VI, endonuclease VIII, Escherichia coli endonuclease III, EXO-3, ExoA, ExoA type AP endonuclease, ExoIII, HAP-1, HAP1, HAP1h, hAPE, hAPE1, hNTH, hNTH1, hOgg1 protein, HpXth, human apurinic/apyrimidinic endonuclease, human apurinic/apyrimidinic endonuclease 1, Kae1, KsgA, LplExo, Micrococcus luteus UV endonuclease, MJ0724, mjOgg, MMH, More, mtAPE, MtbXthA, multi-functional apyrimidinic endonuclease1/redox factor-1, N-glycosylase AP lyase, N-glycosylase apurinic/apyrimidinic lyase, NapE, Nei, Nfo, Ntg1, Ntg1p, Ntg2, Ntg2p, Nth, NTH1, nuclease SmnA, nuclease, apurinic endodeoxyribo-, nuclease, apurinic-apyrimidinic endodeoxyribo-, nuclease, endodeoxyribo-, III, Ogg2, oxoG DNA glycosylase, Pa-AGOG, Pa-AGOG DNA glycosylase, PAE2237, PaKae1, PALF, pE296R, PF0258, phage-T4 UV endonuclease, redox effector factor 1, redox factor-1, redox factor-1:Ref-1, Ref-1, REF-1 protein, Ref1, SisExoIII, Smx nuclease, TvoExo, UL30, UV endo V, UV endonuclease, UV endonuclease V, X-ray endonuclease III, XTH, xthA, ZAP1, zApe

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.99 Other carbon-oxygen lyases
                4.2.99.18 DNA-(apurinic or apyrimidinic site) lyase

Crystallization

Crystallization on EC 4.2.99.18 - DNA-(apurinic or apyrimidinic site) lyase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
V217G variant is crystallized with decamer dsDNA molecule, and the three-dimensional structure is determined to 1.7 A resolution
crystals of zApe (74 mg/ml in 10 mM HEPES, pH 7.5 buffer) are grown by hanging drop vapor diffusion at 20°C using 200 mM ammonium acetate, 100 mM Bis-Tris pH 5.5, 7% PEG 3350, 2% glycerol and 0.8 mM lead acetate as the precipitating solution. The structure is solved at a resolution of 49.15-2.3 A
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combination of dialysis and seeding techniques, sitting drop vapor diffusion method
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Crystals are grown by vapor diffusion. The 1.10-A resolution DNA-free and the 2.45-A resolution DNA-substrate complex structures capture substrate stabilization by Arg37 and reveal a distorted Zn3-ligand arrangement that reverts, after catalysis, to an ideal geometry suitable to hold rather than release cleaved DNA product. Coordinates and structure factors for the three structures (E261Q-phosphate, E261Q-AP DNA and Y72A-AP DNA) have been deposited with accession codes 2NQH, 2NQJ and 2NQ9
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to 1.6 A resolution
molecular modeling of inhibitors to crystal structure, PDB entry 1DE8
mutant C65A hApe1 protein is diluted to 10 mg/ml in 10 mM HEPES pH 7.5 and then crystallized by hanging drop vapor diffusion using 10 mM MES pH 6.0, 7.5 mM Sm(OAc)3, 4% dioxane, 10-20% PEG 8000 as the precipitating solution at 20°C. The structure is solved at a resolution of 33.0-1.9 A
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to 1.92 A resolution with a single Mg2+ ion in the active site. The structure reveals ideal octahedral coordination of Mg2+ via two carboxylate groups and four water molecules. One residue that coordinates Mg2+ directly and two that bind inner-sphere water molecules are strictly conserved in the DNase I superfamily
X-ray diffraction analysis of APE1 complexes with oligomeric DNA-duplexes (11 or 15 bp) containing an AP site. There is only one bivalent metal ion in the APE1 active site present in the crystal formed at pH 4.6. In the structure produced at pH 7.5, i.e. under conditions optimal for endonuclease activity, two metal ions are located in the active site of the enzyme
crystals are produced in hanging drops, the structure is solved at a resolution of 2.5 A
hanging-drop, vapor-diffusion method at 12°C. A single crystal of the mutant enzyme K129Q in complex with a 15-mer duplex DNA oligonucleotide containing 8-oxoG paired with C is used to collect a 2.7 A data
the crystal structure of NMB2082/NApe is solved at a 1.5 A resolution
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crystal structure of the enzyme and that of its complex with 8-oxo-guanosine at 1.0 and 1.7 A resolution, respectively, are grown by sitting drops method
structures are deposited into the Brookhaven Protein Data Bank under the accession numbers 2IVN, 2IVO and 2IVP, structure is solved to 3.0 A and further refined to 1.6 A
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purified enzyme, sitting drop vapor diffusion method, a single crystal is obtained from 0.1 M bicine, pH 9.0, with 20% PEG 6000, at 16°C, X-ray diffraction structure determination and analysis, molecular replacement using the structure of Bacillus subtilis AP endonuclease ExoA (PDB ID 5CFE) as template
molecular modeling of structure, based on the homology to the human enzyme
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