Comparative Kinetic Studies on the Two Interconvertible Forms of Streptococcus Faecalis Inorganic Pyrophosphatase

Overview

Journal Biochem J

Specialty Biochemistry

Date 1985 Oct 15

PMID 2998349

Citations 2

Authors

R Lahti

H Lonnberg

Affiliations

Soon will be listed here.

Abstract

In this work the two interconvertible forms of inorganic pyrophosphatase (EC 3.6.1.1) of Streptococcus faecalis were shown to differ in kinetics. The highly active form of the enzyme was more sensitive to the changes in the Mg2+ concentration, and thus also more sensitive to the inhibition caused by ATP, which competes with PPi for the chelation of Mg2+ ions. We have previously described a kinetic model for the less-active form of S. faecalis inorganic pyrophosphatase [Lahti & Jokinen (1985) Biochemistry 24, 3526-3530]. The kinetic model of the highly active enzyme form is proposed to be a modification of the model of the less-active form in which enzyme activation by free Mg2+ is necessary for the reaction to occur. In this model the enzyme exists in two states, referred to as R- and T-states. In the absence of ligands the enzyme is in the T-state. R-state, i.e. the catalytically active state, exists only in the presence of free Mg2+. Mg1PPi2- is the primary substrate, and free pyrophosphate is a weak inhibitor that cannot serve as a substrate for the highly active form of S. faecalis inorganic pyrophosphatase. This model closely resembles that previously presented for yeast inorganic pyrophosphatase.

Citing Articles

Substrate kinetics of the tonoplast h-translocating inorganic pyrophosphatase and its activation by free mg.

White P, Marshall J, Smith J Plant Physiol. 1990; 93(3):1063-70.

PMID: 16667558 PMC: 1062631. DOI: 10.1104/pp.93.3.1063.

Effects of spermine and spermidine on the inorganic pyrophosphatase of Streptococcus faecalis. Interactions between polyamines and inorganic pyrophosphate.

Lahti R, Hannukainen R, Lonnberg H Biochem J. 1989; 259(1):55-9.

PMID: 2541687 PMC: 1138472. DOI: 10.1042/bj2590055.

References

Kukko E, Heinonen J . The intracellular concentration of pyrophosphate in the batch culture of Escherichia coli. Eur J Biochem. 1982; 127(2):347-9. DOI: 10.1111/j.1432-1033.1982.tb06878.x. View

Brotcorn A, Caillet-Fauquet P, Diver W, Dohet C, Doubleday O, Lecomte P . Conservation and diversification of genes by mismatch correction and SOS induction. Biochimie. 1982; 64(8-9):559-64. DOI: 10.1016/s0300-9084(82)80087-4. View

Lahti R, Jokinen M . Kinetic model for the action of the inorganic pyrophosphatase from Streptococcus faecalis. Biochemistry. 1985; 24(14):3526-30. DOI: 10.1021/bi00335a021. View

Albert A . Quantitative studies of the avidity of naturally occurring substances for trace metals. II. Amino-acids having three ionizing groups. Biochem J. 1952; 50(5):690-7. PMC: 1197727. DOI: 10.1042/bj0500690. View

MONOD J, Wyman J, Changeux J . ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. J Mol Biol. 1965; 12:88-118. DOI: 10.1016/s0022-2836(65)80285-6. View

Klemme J, Gest H . Regulatory properties of an inorganic pyrophosphatase from the photosynthic bacterium Rhodospirillum rubrum. Proc Natl Acad Sci U S A. 1971; 68(4):721-5. PMC: 389028. DOI: 10.1073/pnas.68.4.721. View

Rapoport T, Hohne W, Reich J, HEITMANN P, RAPOPORT S . A kinetic model for the action of the inorganic pyrophosphatase from bakers' yeast. The activating influence of magnesium ions. Eur J Biochem. 1972; 26(2):237-46. DOI: 10.1111/j.1432-1033.1972.tb01761.x. View

MOE O, Butler L . Yeast inorganic pyrophosphatase. II. Kinetics of Mg 2+ activation. J Biol Chem. 1972; 247(22):7308-14. View

PELLER L . On the free-energy changes in the synthesis and degradation of nucleic acids. Biochemistry. 1976; 15(1):141-6. DOI: 10.1021/bi00646a021. View

10.

Heinonen J, Joronen I, Tuokko H . Adaptation of the cells of Escherichia coli to the presence of hydroxyurea increases the level of inorganic pyrophosphatase acttivity. Chem Biol Interact. 1976; 12(1):91-8. DOI: 10.1016/0009-2797(76)90070-3. View

11.

Klemme J . Regulation of intracellular pyrophosphatase-activity and conservation of the phosphoanhydride-energy of inorganic pyrophosphate in microbial metabolism. Z Naturforsch C Biosci. 1976; 31(9-10):544-50. DOI: 10.1515/znc-1976-9-1011. View

12.

Heinonen J, Kukko E . Partial inhibition of DNA synthesis gives rise to increase in the level of inorganic pyrophosphatase in the growing cells of Escherichia coli. Chem Biol Interact. 1977; 17(1):113-6. DOI: 10.1016/0009-2797(77)90076-x. View

13.

Dignam J, Deutscher M . Aminoacyl-tRNA synthetase stimulatory factors and inorganic pyrophosphatase. Biochemistry. 1979; 18(14):3165-70. DOI: 10.1021/bi00581a039. View

14.

Herbomel P, Ninio J . [Fidelity of a polymerization reaction according to the proximity to equilibrium]. C R Seances Acad Sci D. 1980; 291(11):881-4. View

15.

Lahti R, Heinonen J . Reversible changes in the activity of inorganic pyrophosphatase of Streptococcus faecalis. The effect of compounds containing SH-groups. Acta Chem Scand B. 1981; 35(1):33-8. DOI: 10.3891/acta.chem.scand.35b-0033. View

16.

Lahti R, Niemi T . Purification and some properties of inorganic pyrophosphatase from Streptococcus faecalis. J Biochem. 1981; 90(1):79-85. DOI: 10.1093/oxfordjournals.jbchem.a133471. View

17.

Lahti R, Heinonen J . Activity changes of inorganic pyrophosphatase of Streptococcus faecalis during batch culture. J Gen Microbiol. 1981; 125(1):185-8. DOI: 10.1099/00221287-125-1-185. View

18.

Lahti R, Suonpaa M . Role of glutathione in the regulation of inorganic pyrophosphatase activity in Streptococcus faecalis. J Gen Microbiol. 1982; 128(5):1023-6. DOI: 10.1099/00221287-128-5-1023. View

19.

Lahti R . Microbial inorganic pyrophosphatases. Microbiol Rev. 1983; 47(2):169-78. PMC: 281570. DOI: 10.1128/mr.47.2.169-178.1983. View