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We explore the principles of pressure tolerance in enzymes of deep‐sea fishes using lactate dehydrogenases (LDH) as a case study. We compared the effects of pressure on the activities of LDH from hadal snailfishes  Notoliparis kermadecensis  and  Pseudoliparis swirei  with those from a shallow‐adapted  Liparis florae  and an abyssal grenadier  Coryphaenoides armatus . We then quantified the LDH content in muscle homogenates using mass‐spectrometric determination of the LDH‐specific conserved peptide LNLVQR. Existing theory suggests that adaptation to high pressure requires a decrease in volume changes in enzymatic catalysis. Accordingly, evolved pressure tolerance must be accompanied with an important reduction in the volume change associated with pressure‐promoted alteration of enzymatic activity (   Δ   V  PP∘). Our results suggest an important revision to this paradigm. Here, we describe an opposite effect of pressure adaptation—a substantial increase in the absolute value of    Δ   V  PP∘in deep‐living species compared to shallow‐water counterparts. With this change, the enzyme activities in abyssal and hadal species do not substantially decrease their activity with pressure increasing up to 1–2 kbar, well beyond full‐ocean depth pressures. In contrast, the activity of the enzyme from the tidepool snailfish,  L. florae , decreases nearly linearly from 1 to 2500 bar. The increased tolerance of LDH activity to pressure comes at the expense of decreased catalytic efficiency, which is compensated with increased enzyme contents in high‐pressure‐adapted species. The newly discovered strategy is presumably used when the enzyme mechanism involves the formation of potentially unstable excited transient states associated with substantial changes in enzyme–solvent interactions.

the febs journal

Pressure tolerance of deep‐sea enzymes can be evolved through increasing volume changes in protein transitions: a study with lactate dehydrogenases from abyssal and hadal fishes