Biochemistry (Moscow), volume 85, issue 3, pages 326-333

Effect of Structure Variations in the Inter-subunit Contact Zone on the Activity and Allosteric Regulation of Inorganic Pyrophosphatase from Mycobacterium tuberculosis

Publication typeJournal Article
Publication date2020-03-22
Quartile SCImago
Q2
Quartile WOS
Q3
Impact factor2.8
ISSN00062979, 16083040
Biochemistry
General Medicine
Abstract
Hexameric inorganic pyrophosphatase from Mycobacterium tuberculosis (Mt-PPase) has a number of structural and functional features that distinguish it from homologous enzymes widely occurring in living organisms. In particular, it has unusual zones of inter-subunit contacts and lacks the N-terminal region common for other PPases. In this work, we constructed two mutant forms of the enzyme, Ec-Mt-PPase and R14Q-Mt-PPase. In Ec-Mt-PPase, the missing part of the polypeptide chain was compensated with a fragment of PPase from Escherichia coli (Ec-PPase). In R14Q-Mt-PPase, a point mutation was introduced to the contact interface between the two trimers of the hexamer. Both modifications significantly improved the catalytic activity of the enzyme and abolished its inhibition by the cofactor (Mg2+ ion) excess. Activation of Mt-PPase by low (∼10 µM) concentrations of ATP, fructose-1-phosphate, L-malate, and non-hydrolyzable substrate analogue methylene bisphosphonate (PCP) was observed. At concentrations of 100 µM and higher, the first three compounds acted as inhibitors. The activating effect of PCP was absent in both mutant forms, and the inhibitory effect of fructose-1-phosphate was absent in Ec-Mt-PPase. The effects of other modulators varied only quantitatively among the mutants. The obtained data indicate the presence of allosteric sites in Mt-PPase, which are located in the zones of inter-subunit contact or associated with them.

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Romanov R. S. et al. Effect of Structure Variations in the Inter-subunit Contact Zone on the Activity and Allosteric Regulation of Inorganic Pyrophosphatase from Mycobacterium tuberculosis // Biochemistry (Moscow). 2020. Vol. 85. No. 3. pp. 326-333.
GOST all authors (up to 50) Copy
Romanov R. S., Kurilova S. A., Baykov A. A., Rodina E. Effect of Structure Variations in the Inter-subunit Contact Zone on the Activity and Allosteric Regulation of Inorganic Pyrophosphatase from Mycobacterium tuberculosis // Biochemistry (Moscow). 2020. Vol. 85. No. 3. pp. 326-333.
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TY - JOUR
DO - 10.1134/S0006297920030086
UR - https://doi.org/10.1134%2FS0006297920030086
TI - Effect of Structure Variations in the Inter-subunit Contact Zone on the Activity and Allosteric Regulation of Inorganic Pyrophosphatase from Mycobacterium tuberculosis
T2 - Biochemistry (Moscow)
AU - Romanov, R S
AU - Kurilova, S. A.
AU - Baykov, A. A.
AU - Rodina, E.V
PY - 2020
DA - 2020/03/22 00:00:00
PB - Pleiades Publishing
SP - 326-333
IS - 3
VL - 85
SN - 0006-2979
SN - 1608-3040
ER -
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@article{2020_Romanov
author = {R S Romanov and S. A. Kurilova and A. A. Baykov and E.V Rodina},
title = {Effect of Structure Variations in the Inter-subunit Contact Zone on the Activity and Allosteric Regulation of Inorganic Pyrophosphatase from Mycobacterium tuberculosis},
journal = {Biochemistry (Moscow)},
year = {2020},
volume = {85},
publisher = {Pleiades Publishing},
month = {mar},
url = {https://doi.org/10.1134%2FS0006297920030086},
number = {3},
pages = {326--333},
doi = {10.1134/S0006297920030086}
}
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Romanov, R. S., et al. “Effect of Structure Variations in the Inter-subunit Contact Zone on the Activity and Allosteric Regulation of Inorganic Pyrophosphatase from Mycobacterium tuberculosis.” Biochemistry (Moscow), vol. 85, no. 3, Mar. 2020, pp. 326-333. https://doi.org/10.1134%2FS0006297920030086.
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