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.
Original language | English |
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Pages (from-to) | 236-238 |
Number of pages | 3 |
Journal | Bioscience, Biotechnology and Biochemistry |
Volume | 79 |
Issue number | 2 |
DOIs | |
Publication status | Published - 2015 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry