Allosteric transitions of rabbit skeletal muscle lactate dehydrogenase induced by pH-dependent dissociation of the tetrameric enzyme

Iacovino, L.G.; Rossi, Michele; Stefano, Giuseppina Di; Rossi, Valentina; Binda, Claudia; Brigotti, Maurizio; Tomaselli, F; Pasti, A P; Piaz, Fabrizio Dal; Cerini, Stefano; Hochkoeppler, Alejandro

doi:10.1016/j.biochi.2022.03.008

Cited by 16 publications

(10 citation statements)

References 69 publications

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“…When the concentration of lactate was high, the slope of the straight line increases rst and then tends to be at, which conforms to the characteristics of Michaelis Menten kinetics [34]. Michaelis-Menten constant ( ) was an important parameter to reveal the kinetics of enzyme substrate reaction [35].This parameter was calculated by Lineweaver Burk Eq.…”

Section: Performances Of Ldh/rgo-cnt/tmc Bioanodesupporting

confidence: 56%

Wearable cellulose textile matrix self-powered biosensor sensing lactate in human sweat

夏,

Zuo,

et al. 2023

Preprint

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A lactate self-powered biosensor was assembled for the detection of lactate in sweat based on flexible textile matrix enzymatic electrodes. A porous three-dimensional electrode with high flexibility and electrical conductivity was obtained by decorating composites of reduced graphene oxide and carboxylate multi-walled carbon nanotubes onto a cellulose fabric substrate. The excellent enzyme embedding method using gel electrolyte showed a Michaelis-Menten constant of 1.46 mM, which implies that lactate dehydrogenase had a high enzymatic activity. The assembled self-powered lactate biosensor showed a sensitivity of 3.16 µW mM− 1 cm− 2 in the 0–10 mM linear range and a detection limit of 9.49 µM (S/N = 3). Meanwhile, the biosensor has good tensile flexural stability, selectivity, and long-term stability. The lactate self-powered biosensor recovered 99.66–108.43% of lactate from real sweat with a relative standard deviation of less than 4.65% when integrated into clothing. The biosensor is promising for sensing lactate in real sweat.

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Section: Performances Of Ldh/rgo-cnt/tmc Bioanodesupporting

confidence: 56%

Wearable cellulose textile matrix self-powered biosensor sensing lactate in human sweat

夏,

Zuo,

et al. 2023

Preprint

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“…The nonallosteric properties of vertebrate LDHs have been recently challenged ( Iacovino et al 2022 ; Pasti et al 2022 ). By recording pyruvate saturation profiles, it was found that their hyperbolic shapes turned sigmoidal when measurements were done at low pH values (pH 5), a phenomenon due to the pH-dependent dissociation of the tetramer into dimeric species.…”

Section: Resultsmentioning

confidence: 99%

“…In fact, using biophysical and molecular dynamic simulations, it has been shown that the LDH-M from the rabbit displays some reminiscent allosteric properties ( Katava et al 2017 ). More recently, it has been shown that rabbit LDH-M and human LDH-M undergo allosteric transition under mildly acidic conditions ( Iacovino et al 2022 ; Pasti et al 2022 ).…”

Section: Introductionmentioning

confidence: 99%

Deciphering Evolutionary Trajectories of Lactate Dehydrogenases Provides New Insights into Allostery

Robin,

Brochier-Armanet,

Bertrand

et al. 2023

Molecular Biology and Evolution

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Lactate dehydrogenase (LDH, EC.1.1.127) is an important enzyme engaged in the anaerobic metabolism of cells, catalyzing the conversion of pyruvate to lactate and NADH to NAD +. LDH is a relevant enzyme to investigate structure-function relationships. The present work provides the missing link in our understanding of the evolution of LDHs. This allows to explain i) the various evolutionary origins of LDHs in eukaryotic cells and their further diversification, as well as ii) subtle phenotypic modifications with respect to their regulation capacity. We identified a group of cyanobacterial LDHs displaying eukaryotic-like LDH sequence features. The biochemical and structural characterization of Cyanobacterium aponinum LDH, taken as representative, unexpectedly revealed that it displays homotropic and heterotropic activation, typical of an allosteric enzyme, whereas it harbors a long N-terminal extension, a structural feature considered responsible for the lack of allosteric capacity in eukaryotic LDHs. Its crystallographic structure was solved in two different configurations typical of the R-active and T-inactive states encountered in allosteric LDHs. Structural comparisons coupled with our evolutionary analyses helped to identify two amino acid positions that could have had a major role in the attenuation and extinction of the allosteric activation in eukaryotic LDHs rather than the presence of the N-terminal extension. We tested this hypothesis by site-directed mutagenesis. The resulting Cyanobacterium aponinum LDH mutants displayed reduced allosteric capacity mimicking those encountered in plants and human LDHs. This study provides a new evolutionary scenario of LDHs that unifies descriptions of regulatory properties with structural and mutational patterns of these important enzymes.

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“…As shown in Figure 2 B, compared with the control, H 2 O 2 significantly ( p < 0.01) reduced the cell viability; then, PSP2-1 significantly increased the cell viability. Lactate dehydrogenase (LDH) is a glycolytic enzyme, which widely exists in the cytoplasm of all tissues or cells in the body [ 28 , 29 ]. When the cells are necrotic and apoptotic, the membrane structure is destroyed, which leads to the release of LDH from the cells.…”

Section: Resultsmentioning

confidence: 99%

Structural Characterization of a Pleurotus sajor-caju Polysaccharide and Its Neuroprotection Related to the Inhibition of Oxidative Stress

et al. 2022

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A novel polysaccharide PSP2-1 was isolated and purified from Pleurotus sajor-caju. The structural characterization data displayed that the molecular weight of PSP2-1 was 44.9 kDa, and PSP2-1 consisted of fucose, galactose, glucose, and mannose. The methylation results showed that the glycosidic bonds of PSP2-1 included T-Fuc, 1,6-Gal, T-Glc, 1,6-Glc, 1,3,6-Glc, 1,3-Man, 1,2,6-Man, and T-Man. Neuroprotective studies indicated that PSP2-1 significantly improved the cell viability of the H2O2-induced oxidatively damaged neuronal cell HT22, reduced the release of LDH, inhibited apoptosis and release of cytochrome c, and alleviated the decline of mitochondrial membrane potential and ROS accumulation. Furthermore, PSP2-1 decreased the phosphorylation levels of cleaved PARP and cleaved caspase-3, and increased the ratio of bcl-2/bax. Additionally, PSP2-1 could inhibit the phosphorylation of MAPK family members including JNK, p38, and Erk. Finally, animal experiments showed that PSP2-1 could improve the oxidative stress injury and the learning and memory ability of mice with aging induced by D-galactose. Our results confirmed that PSP2-1 significantly ameliorated the oxidative stress injury, inhibited the apoptosis in H2O2-induced neuronal cells via MAPK pathway, and also improved cognition in mice with aging induced by D-galactose. Our research gives the foundation for the functional food application of P. sajor-caju polysaccharides in the future.

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Allosteric transitions of rabbit skeletal muscle lactate dehydrogenase induced by pH-dependent dissociation of the tetrameric enzyme

Cited by 16 publications

References 69 publications

Wearable cellulose textile matrix self-powered biosensor sensing lactate in human sweat

Wearable cellulose textile matrix self-powered biosensor sensing lactate in human sweat

Deciphering Evolutionary Trajectories of Lactate Dehydrogenases Provides New Insights into Allostery

Structural Characterization of a Pleurotus sajor-caju Polysaccharide and Its Neuroprotection Related to the Inhibition of Oxidative Stress

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