Roles of Ala-149 in the catalytic activity of diadenosine tetraphosphate phosphorylase from Mycobacterium tuberculosis H37Rv.
Diadenosine 5',5'''-P(1),P(4)-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'''-P(1),P(5)-pentaphosphate and was inactive on Ap4A and other substrates that are utilized by the wild-type enzyme.
['Mori|Shigetarou|S|', 'Kim|Hyun|H|', 'Rimbara|Emiko|E|', 'Arakawa|Yoshichika|Y|', 'Shibayama|Keigo|K|']
D000409:Alanine D000595:Amino Acid Sequence D055162:Biocatalysis D020134:Catalytic Domain D008958:Models, Molecular D008969:Molecular Sequence Data D009169:Mycobacterium tuberculosis D009713:Nucleotidyltransferases
phosphorylase drug target kinetics mycobacteria