Journal
PROTEIN EXPRESSION AND PURIFICATION
Volume 112, Issue -, Pages 37-42Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2015.04.010
Keywords
Nontuberculous mycobacteria; Nucleotide phosphorylase; Kinetics; Drug target
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Funding
- Ministry of Health, Labour and Welfare of Japan [H25-Shinkou-Ippan-005, H24-Shinkou-Ippan-010]
- Ministry of Education, Culture, Sports, Science and Technology of Japan [24780088]
- Grants-in-Aid for Scientific Research [24780088, 23790490, 25860329, 15K07377] Funding Source: KAKEN
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We recently demonstrated that the Rv2613c protein from Mycobacterium tuberculosis H37Rv is a novel diadenosine 5',5'-P-1,P-4-tetraphosphate (Ap(4)A) phosphorylase (MtAPA) that forms a tetramer. Mycobacterium avium and Mycobacterium smegmatis express proteins named MAV_3489 and MSMEG_2932, respectively, that are homologous to MtAPA. Here we showed that the MAV_3489 and MSMEG_2932 proteins possess Ap(4)A phosphorylase activity and enzymatic properties similar to those of MtAPA. Furthermore, gel-filtration column chromatography revealed that MAV_3489 and MSMEG_2932 assembled into homotetramers in solution, indicating that they may also form unique Ap(4)A-binding sites composed of tetramers. (C) 2015 Elsevier Inc. All rights reserved.
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