Roles of Ala-149 in the catalytic activity of diadenosine tetraphosphate phosphorylase from Mycobacterium tuberculosis H37Rv

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Abstract

Diadenosine 5′,5′′′-P1,P4-tetraphosphate (Ap4A) phosphorylase from Mycobacterium tuberculosis 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′′ ′-P1,P5-pentaphosphate and was inactive on Ap4A and other substrates that are utilized by the wild-type enzyme.

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Mori, S., Kim, H., Rimbara, E., Arakawa, Y., & Shibayama, K. (2015). Roles of Ala-149 in the catalytic activity of diadenosine tetraphosphate phosphorylase from Mycobacterium tuberculosis H37Rv. Bioscience, Biotechnology and Biochemistry, 79(2), 236–238. https://doi.org/10.1080/09168451.2014.973364

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