An essential tyrosine residue of Aspergillus polygalacturonase

FEBS Letters
E StratilováH Jörnvall

Abstract

Based on strict conservation of a tyrosine residue in 24 polygalacturonases, tyrosine modification was assessed in two different forms of the Aspergillus enzyme. The second subform was unknown in structure but submitted to sequence analysis and was found also to have the conserved tyrosine residue. Results of chemical modifications are consistent in showing inactivation of the proteins with all tyrosine-reactive agents tested, acetic anhydride, N-acetyl imidazole, and tetranitromethane. Furthermore, after acetylation, regeneration of enzyme activity was possible with hydroxylamine. Spectrophotometric pH titration showed that one accessible tyrosine residue is ionized at pH 9.3-9.5, whereas the remaining, masked residues are all ionized at pH 10.5. It is concluded that one tyrosine residue is catalytically important, in agreement with the inactivation and reactivation data, that this residue is accessible, and that it is likely to correspond to the strictly conserved residue observed in all forms.

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Citations

Sep 18, 2004·International Journal of Biological Macromolecules·A A SabouryB Farzami
Mar 22, 2008·Genome Génome / Conseil National De Recherches Canada·K-C ParkN-S Kim
May 7, 2004·The Journal of Immunology : Official Journal of the American Association of Immunologists·Ines SwobodaSusanne Spitzauer
Jun 25, 1998·Plant Physiology·K A Hadfield, A B Bennett
Nov 13, 2004·Biochimica Et Biophysica Acta·Kamahldin HaghbeenFarhad Karbassi

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