| First Author | Grin IR | Year | 2010 |
| Journal | Biochem Biophys Res Commun | Volume | 394 |
| Issue | 1 | Pages | 100-5 |
| PubMed ID | 20175991 | Mgi Jnum | J:158820 |
| Mgi Id | MGI:4440685 | Doi | 10.1016/j.bbrc.2010.02.121 |
| Citation | Grin IR, et al. (2010) Inactivation of NEIL2 DNA glycosylase by pyridoxal phosphate reveals a loop important for substrate binding. Biochem Biophys Res Commun 394(1):100-5 |
| abstractText | Pyridoxal-5'-phosphate (PLP), in addition to its known metabolic functions, inactivates many DNA-dependent enzymes through conjugation to their critical amino groups. We have investigated the ability of PLP to inhibit bifunctional DNA repair glycosylases, which possess a catalytic amine. Of six enzymes tested, only endonuclease VIII-like protein 2 (NEIL2) was significantly inhibited by PLP. The inhibition was due to Schiff base formation between PLP and the enzyme. PLP-conjugated NEIL2 completely lost its ability to bind damaged DNA. Liquid chromatography/nanoelectrospray ionization tandem mass spectrometry of the products of proteolysis of pyridoxylated NEIL2 identified Lys50 as the site of modification. Thus, the beta2/beta3 loop where Lys50 is located in NEIL2 is important for DNA binding, presumably lies next to a phosphate-binding site, and may represent a target for regulation of the enzyme activity. |
