Hofmeister effect on catalytic properties of chymotrypsin is substrate-dependent

Dušeková, Eva; Garajová, Katarína; Yavaşer, Rukiye; Varhač, Rastislav; Sedlák, Erik

doi:10.1016/j.bpc.2018.10.002

Cited by 15 publications

(17 citation statements)

References 80 publications

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“…This agrees with previous ambient pressure studies showing the same effect of perchlorate salts on α-CT and other enzymes 7 , 13 . Furthermore, the observation that MgSO 4 increases the activity of α-CT agrees with previous studies which show that the sulphate ion can stabilise proteins 14 and increase the activity of α-CT 15 . This sulphate-induced effect is also shown to be substrate dependent as it was absent in a previous kinetic study using N -benzoyl- L -tyrosine ethyl ester as the substrate.…”

Section: Discussionsupporting

confidence: 91%

“…Previous studies have demonstrated the deleterious effects of destabilising ions such as perchlorates on the activity of α-chymotrypsin (α-CT) and other enzymes 7 , 13 . Conversely, stabilising salts, such as sodium sulphate 14 , have been shown to increase the activity and structural stability of α-CT 15 . Our knowledge of how these molecules affect enzyme activity is largely restricted to ambient temperatures and pressures.…”

Section: Introductionmentioning

confidence: 99%

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High pressures increase α-chymotrypsin enzyme activity under perchlorate stress

et al. 2020

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Deep subsurface environments can harbour high concentrations of dissolved ions, yet we know little about how this shapes the conditions for life. We know even less about how the combined effects of high pressure influence the way in which ions constrain the possibilities for life. One such ion is perchlorate, which is found in extreme environments on Earth and pervasively on Mars. We investigated the interactions of high pressure and high perchlorate concentrations on enzymatic activity. We demonstrate that high pressures increase α-chymotrypsin enzyme activity even in the presence of high perchlorate concentrations. Perchlorate salts were shown to shift the folded α-chymotrypsin phase space to lower temperatures and pressures. The results presented here may suggest that high pressures increase the habitability of environments under perchlorate stress. Therefore, deep subsurface environments that combine these stressors, potentially including the subsurface of Mars, may be more habitable than previously thought.

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Section: Discussionsupporting

confidence: 91%

Section: Introductionmentioning

confidence: 99%

High pressures increase α-chymotrypsin enzyme activity under perchlorate stress

et al. 2020

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“…The correlations between the intrinsic properties of anions and the properties of HRV 3C protease suggest that (i) stabilization effect of anions depends on the charge density of anions, and (ii) the catalytic properties of the enzyme is dependent on the viscosity Bcoefficient of the anions (Figure 6). In our previous works, we showed for several independent proteins such as cytochrome c, apoflavodoxin, chymotrypsin and lysozyme a relation between charge density of anions and stability of the proteins [4,51,58].…”

Section: Modulation Of Hrv 3c Protease Properties By Specific Anion E...mentioning

confidence: 96%

Specific anion effect on properties of HRV 3C protease

Dušeková

Berta²,

Sedláková³

et al. 2022

Biophysical Chemistry

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“…Chaotropic salts are normally associated with deleterious phenomena such as reduced enzyme activity and protein stability 3 , 13 – 16 , whereas kosmotropic salts normally produce the opposite effect 17 , 18 . However, this representation is an oversimplification as it is possible to find examples where kosmotropic salts decrease enzyme activity 19 and examples where highly chaotropic agents increase enzyme activity 19 – 32 .…”

Section: Introductionmentioning

confidence: 99%

“…Here we use α-chymotrypsin as a model enzyme to explore the effects of perchlorate salts on enzyme activity across temperature. Bovine α-chymotrypsin is a standard serine protease which is mesophilic with regards to its temperature stability and has been shown to exhibit reduced activity and structural stability in the presence of chaotropic molecules such as perchlorate and thiocyanate salts 3 , 13 , 15 , 17 , whereas kosmotropic molecules such as NaSO 4 has previously been shown to increase α-chymotrypsin’s activity and stability 17 . We show here that Mg(ClO 4 ) 2 and NaClO 4 lower the enzyme activity of α-chymotrypsin at room temperature, but that at lower temperatures these salts become activators of enzyme activity.…”

Section: Introductionmentioning

confidence: 99%

Perchlorate salts confer psychrophilic characteristics in α-chymotrypsin

Gault

Jaworek

Winter

et al. 2021

Sci Rep

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Studies of salt effects on enzyme activity have typically been conducted at standard temperatures and pressures, thus missing effects which only become apparent under non-standard conditions. Here we show that perchlorate salts, which are found pervasively on Mars, increase the activity of α-chymotrypsin at low temperatures. The low temperature activation is facilitated by a reduced enthalpy of activation owing to the destabilising effects of perchlorate salts. By destabilising α-chymotrypsin, the perchlorate salts also cause an increasingly negative entropy of activation, which drives the reduction of enzyme activity at higher temperatures. We have also shown that α-chymotrypsin activity appears to exhibit an altered pressure response at low temperatures while also maintaining stability at high pressures and sub-zero temperatures. As the effects of perchlorate salts on the thermodynamics of α-chymotrypsin’s activity closely resemble those of psychrophilic adaptations, it suggests that the presence of chaotropic molecules may be beneficial to life operating in low temperature environments.

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Hofmeister effect on catalytic properties of chymotrypsin is substrate-dependent

Cited by 15 publications

References 80 publications

High pressures increase α-chymotrypsin enzyme activity under perchlorate stress

High pressures increase α-chymotrypsin enzyme activity under perchlorate stress

Specific anion effect on properties of HRV 3C protease

Perchlorate salts confer psychrophilic characteristics in α-chymotrypsin

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