Roles of Ala-149 in the catalytic activity of diadenosine tetraphosphate phosphorylase from <i>Mycobacterium tuberculosis</i> H37Rv Shigetarou Mori Hyun Kim Emiko Rimbara Yoshichika Arakawa Keigo Shibayama 10.6084/m9.figshare.1310470.v4 https://tandf.figshare.com/articles/presentation/Roles_of_Ala_149_in_the_catalytic_activity_of_diadenosine_tetraphosphate_phosphorylase_from_i_Mycobacterium_tuberculosis_i_H37Rv/1310470 <div><p>Diadenosine 5′,5′′′-<i>P</i><sup>1</sup>,<i>P</i><sup>4</sup>-tetraphosphate (Ap<sub>4</sub>A) phosphorylase from <i>Mycobacterium tuberculosis</i> H37Rv (MtAPA) belongs to the histidine triad motif (HIT) superfamily, but is the only member with an alanine residue at position 149 (Ala-149). Enzymatic analysis revealed that the Ala-149 deletion mutant displayed substrate specificity for diadenosine 5′,5′′′-<i>P</i><sup>1</sup>,<i>P</i><sup>5</sup>-pentaphosphate and was inactive on Ap<sub>4</sub>A and other substrates that are utilized by the wild-type enzyme.</p></div> 2015-10-08 18:28:48 Mycobacterium tuberculosis H 37Rv position 149 Ap 4A substrate specificity hit histidine triad motif Ap 4A phosphorylase diadenosine tetraphosphate phosphorylase alanine residue ala