The Sabatier principle as a tool for discovery and engineering of industrial enzymes

Kari, Jeppe; Schaller, Kay; Molina, Gustavo A.; Borch, Kim; Westh, Peter

doi:10.1016/j.copbio.2022.102843

Cited by 12 publications

(15 citation statements)

References 32 publications

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“…However, it should be noted that Δ41- La Pul also showed a 14-fold increased k cat compared with La Pul (Table ). The behavior of Δ41- La Pul, which loses affinity for the substrate, while it gains activity can be described as desorption-limited reactions according to the Sabatier principle . The Sabatier principle can be applied to two scenarios: desorption-limited and adsorption-limited reactions .…”

Section: Discussionmentioning

confidence: 99%

“…In contrast to the desorptionlimited situation observed for LaPul and Δ41-LaPul on soluble substrate (pullulan and amylopectin in this work), the reaction of LaPul and Δ41-LaPul on granular starches showed an adsorption-limited situation according to the Sabatier principle. 47 To better understand the observed differences between soluble α-glucan substrates and starch granules, it is important to consider the substrate variation. Glucan chains in solution are very flexible, allowing for easy binding to CBM41 and CD.…”

Section: Effect Of Ntds On Binding To Starch Granulesmentioning

confidence: 99%

“…The behavior of Δ41-LaPul, which loses affinity for the substrate, while it gains activity can be described as desorption-limited reactions according to the Sabatier principle. 47 The Sabatier principle can be applied to two scenarios: desorption-limited and adsorption-limited reactions. 48 In adsorption-limited reactions, a higher affinity between catalyst and substrate leads to higher activity.…”

Section: Effect Of Ntds On Binding To Starch Granulesmentioning

confidence: 99%

See 2 more Smart Citations

Functional Roles of N-Terminal Domains in Pullulanase from Human Gut Lactobacillus acidophilus

Wang,

Svensson,

Henrissat

et al. 2023

J. Agric. Food Chem.

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Section: Discussionmentioning

confidence: 99%

Section: Effect Of Ntds On Binding To Starch Granulesmentioning

confidence: 99%

Section: Effect Of Ntds On Binding To Starch Granulesmentioning

confidence: 99%

See 1 more Smart Citation

Functional Roles of N-Terminal Domains in Pullulanase from Human Gut Lactobacillus acidophilus

Wang,

Svensson,

Henrissat

et al. 2023

J. Agric. Food Chem.

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“…Recently, several studies have provided critical insight on the optimum K m value (6, 7). Kari et al have shown experimentally that the activity of cellulases and poly (ethylene terephthalate) (PET) hydrolases can be maximized when the K m is neither too large nor too small (6, 8, 9).…”

Section: Introductionmentioning

confidence: 99%

Diverse Phosphoserine Phosphatases Exhibit Maximum Activity at an Intermediate Binding Affinity in Accord with the Sabatier Principle of Catalysis

Chiba

Ooka

Wintzer

et al. 2023

Preprint

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A unified framework to rationalize enzymatic activity is essential to understand cellular function and metabolic evolution. Recent studies have shown that the activity of several hydrolases is maximized when the substrate binding affinity (Michaelis-Menten constant: Km) is neither too strong nor too weak. This is because an intermediate Km resolves the trade-off between Km and kcat, in accord with the Sabatier principle of artificial catalysis. However, it remains unclear whether this concept is applicable to enzymes in general, especially for those which catalyze the same reaction but have evolved under different selection pressures due to the phylogeny or physiology of the host organism. Here, we demonstrate that the activity of 10 distinct wild-type phosphoserine phosphatases (PSP) exhibits a maximum at an intermediate binding affinity (Km approximately 0.5 mM), indicating that they also follow the Sabatier principle. Furthermore, by considering not only Km but also the equilibrium rate constant (k20) of each enzyme, we have succeeded in rationalizing the PSP activity quantitatively. k20 is the rate constant of product release (ES to E + P) in the absence of any driving force, and a large k20 allows kcat to be increased without increasing Km. Although the traditional Sabatier principle considers only the binding affinity (Km), we show that the additional contribution of k20 drastically improves the consistency between experiments and theory. Our expanded framework which quantitatively explains the activity of phylogenetically and physiologically diverse enzymes with respect to their physicochemical parameters may lead to the rational design of highly active enzymes.

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“…Notably, in our previous work for lactonase Sso Pox, we observed a similar trend between and SPI . A recent study by Bååth et al showed that the turnover of poly(ethylene terephthalate) hydrolases also follows a valley-shaped trend, , where the turnover rate is initially enhanced and then diminished as the monotonic decrease in enzyme–substrate binding affinity. This kinetic profile is consistent with Sabatier principle.…”

mentioning

confidence: 99%

Substrate Positioning Dynamics Involves a Non-Electrostatic Component to Mediate Catalysis

Jiang,

Ding,

Shao

et al. 2023

J. Phys. Chem. Lett.

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The Sabatier principle as a tool for discovery and engineering of industrial enzymes

Cited by 12 publications

References 32 publications

Functional Roles of N-Terminal Domains in Pullulanase from Human Gut Lactobacillus acidophilus

Functional Roles of N-Terminal Domains in Pullulanase from Human Gut Lactobacillus acidophilus

Diverse Phosphoserine Phosphatases Exhibit Maximum Activity at an Intermediate Binding Affinity in Accord with the Sabatier Principle of Catalysis

Substrate Positioning Dynamics Involves a Non-Electrostatic Component to Mediate Catalysis

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