Lactate dehydrogenase in abdominal muscle of crayfishOrconectes limosus and shrimpcrangon crangon (Decapoda: Crustacea): Properties and evolutionary relationship

̧tara, Marek S. Zie; Gronczewska, Jadwiga; Stachowiak, Krystyna; Skorkowski, Edward F.

doi:10.1016/0305-0491(96)00064-8

Cited by 17 publications

(7 citation statements)

References 23 publications

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“…It is well documented that LDH from most ectothermic animals displays clear substrate inhibition kinetics Baldwin et al, 1989;French and Hochachka, 1978;Narita and Horiuchi, 1979;Place and Powers, 1984;Tsukuda and Yamawaki, 1980;Zietara et al, 1996;Zietara and Skorkowski, 1993), caused by the formation of a covalent adduct between pyruvate and the oxidized form of the cofactor, i.e. the formation of an inhibitory enzyme-NAD + -pyruvate complex (Eszes et al, 1996;Hewitt et al, 1999).…”

Section: Kinetic Studymentioning

confidence: 99%

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Effects of temperature acclimation on lactate dehydrogenase of cod(Gadus morhua): genetic, kinetic and thermodynamic aspects

Zakhartsev

Johansen

Pörtner

et al. 2004

Journal of Experimental Biology

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SUMMARYThe aim of this study was to determine the effects of seasonal temperature variation on the functional properties of lactate dehydrogenase (LDH) from white muscle and liver of Norwegian coastal cod (Gadus morhua) and the possible relevance of LDH allelic variability for thermal acclimation. Two groups of fishes were acclimated to 4°C or 12°C for one year. Polymorphism was observed in only one (Ldh-B) of the three Ldh loci expressed in cod liver and/or muscle. Isozyme expression remained unchanged regardless of acclimation temperature(TA). The products of locus Ldh-B comprise only 14–19% (depending on the tissue) of total LDH activities and,consequently, differences between phenotypes are negligible in terms of their effect on LDH total performance. No kinetic(\batchmode \documentclass[fleqn,10pt,legalpaper]{article} \usepackage{amssymb} \usepackage{amsfonts} \usepackage{amsmath} \pagestyle{empty} \begin{document} \(K_{\mathrm{m}}^{\mathrm{PYR}}\) \end{document}, \batchmode \documentclass[fleqn,10pt,legalpaper]{article} \usepackage{amssymb} \usepackage{amsfonts} \usepackage{amsmath} \pagestyle{empty} \begin{document} \(K_{\mathrm{si}}^{\mathrm{PYR}}\) \end{document}, Vmax) or thermodynamic (Ea,Δ G) differences were found among Ldh-B phenotypes. Clear kinetic differences were observed between LDH isoforms in the two tissues. However, the Arrhenius activation energy (Ea) for pyruvate reduction was the same for both tissues (Ea=47 kJ mol–1) at TA=12°C. Factors TA, tissue and phenotype did not reveal a significant effect on the Gibbs free energy change (ΔG) of the reaction(55.5 kJ mol–1). However, at TA=4°C,the Ea was increased (Ea=53–56 kJ mol–1) and the temperature dependence of the constant of substrate inhibition for pyruvate(\batchmode \documentclass[fleqn,10pt,legalpaper]{article} \usepackage{amssymb} \usepackage{amsfonts} \usepackage{amsmath} \pagestyle{empty} \begin{document} \(K_{\mathrm{si}}^{\mathrm{PYR}}\) \end{document}) decreased in both muscle and liver.In conclusion, the strategies of LDH adjustment to seasonal temperature variations in cod involve changes in LDH concentration (quantitative),adjustment of thermodynamic (Ea) and kinetic(\batchmode \documentclass[fleqn,10pt,legalpaper]{article} \usepackage{amssymb} \usepackage{amsfonts} \usepackage{amsmath} \pagestyle{empty} \begin{document} \(K_{\mathrm{si}}^{\mathrm{PYR}}\) \end{document}) properties of the LDH(modulative) but not the expression of alternative isoforms (qualitative). We assume that the observed increase in Ea and the decrease of temperature dependence of \batchmode \documentclass[fleqn,10pt,legalpaper]{article} \usepackage{amssymb} \usepackage{amsfonts} \usepackage{amsmath} \pagestyle{empty} \begin{document} \(K_{\mathrm{si}}^{\mathrm{PYR}}\) \end{document} at low TA is the result of structural changes of the LDH molecule(temperature-driven protein folding). We propose a new mechanism of metabolic compensation of seasonal temperature variations – cold acclimation results in changes in the kinetic and thermodynamic properties of LDH in a way that favours aerobic metabolism through reduction of the competition of LDH for pyruvate in normoxic conditions.

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Section: Kinetic Studymentioning

confidence: 99%

“…In many fishes, LDH is coded by three independent loci (De Panepucci et al, 1984;Ferreria et al, 1991;Zietara et al, 1996). Simultaneous expression of LDH isozymes (A, B and C) and allozymes of LDH-B yields a complicated electrophoretic pattern (overall LDH suite), which is sometimes difficult to interpret.…”

mentioning

confidence: 99%

Effects of temperature acclimation on lactate dehydrogenase of cod(Gadus morhua): genetic, kinetic and thermodynamic aspects

Zakhartsev

Johansen

Pörtner

et al. 2004

Journal of Experimental Biology

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“…Under aerobic conditions, pyruvate is oxidized to CO2, H2O, and ATP, while under anaerobic conditions LDH reduces pyruvate to L-lactate releasing a small amount of ATP. Thus, LDH is a useful indicator of organisms' capability for anaerobic metabolism (Zietara, Gronczewska, Stachowiak, & Skorkowski, 1996).…”

Section: Discussionmentioning

confidence: 99%

Untitled

Jia¹,

Fan²,

Wang³

et al. 2019

Turk. J. Fish. Aquat. Sci.

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To investigate waterless stress during transport from aquacultures to sale points on the physiological and energy-metabolism properties of Paramisgurnus dabryanus, to improve for improving traditional preservation methods, the levels of glucose, cortisol, triglyceride, and cholesterol in serum and the activities of hexokinase (HK), pyruvate kinase (PK), lactic dehydrogenase (LDH), and succinate dehydrogenase (SDH) in muscle were determined. Chinese loaches were subjected to water, lesswater, and no-water conditions for 8h. Less-water and no-water stress significantly increased cortisol concentration in serum, while triglycerides and total cholesterol levels slightly decreased. In the initial stages of stress, glucose dropped dramatically and then recovered gradually, eventually exceeding that in the control group. The activities of HK, PK, and LDH increased and then decreased. While HK and PK activities were significantly higher at the end than at the beginning of the stress, LDH activity returned to its pre-stress level. Under less-water and no-water stresses, SDH activity first decreased and then increased. Overall, there were no significant differences between less-water and no-water groups in the measured parameters, except SDH, at the end of the experiment, and variations in all parameters were similar. Waterless preservation conditions resulted in acute stress, acute hyperglycemia, and energetic compensation.

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“…In general, it is well documented that LDH from most ectothermic animals displays peculiar kinetic properties characterized by high levels of substrate inhibition [7][8][9][10][11][12][13][14]. This means that, at low substrate concentrations, the reaction follows normal MichaelisMenten kinetics but, when substrate concentrations reach high level, the inhibition sets in.…”

Section: Kineticsmentioning

confidence: 96%

Environmentally low-temperature kinetic and thermodynamic study of lactate dehydrogenase from Atlantic cod (G. morhua) using a 96-well microplate technique

Zakhartsev

Pörtner

Blust

2004

Analytical Biochemistry

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Analyses of temperature-dependent kinetic parameters in enzymes extracted from tissues of ectothermic animals are usually carried out within the range of physiological temperatures (0-40 degrees C). However, multisample spectrophotometers (so-called microplate readers) with efficient wide-range temperature control (including cooling) have previously been unavailable. This limits the statistical quality of the measurements. A temperature-controlled microplate was designed for a 96-well microplate reader to overcome this limitation. This so-called T-microplate is able to control assay temperature between the freezing point of a liquid sample and 60 degrees C with high stability and accuracy in any data acquisition mode. At 4 degrees C the accuracy of the temperature control was +/-0.1 degrees C and temperature homogeneity across the microplate was +/-0.3 degrees C. As examples, analyses of the temperature dependence of Michaelis-Menten (K'(PYR)(m) and substrate inhibition (K'(PYR)(si) constants for pyruvate, of the maximal rate of reaction (V'(max), of the apparent Arrhenius activation energy (E(A), and of the Gibbs free-energy change (deltaG) of lactate dehydrogenases from muscle of Atlantic cod Gadus morhua acclimated to 4 degrees C are described. The large dataset obtained allowed evaluation of a new mechanism of metabolic compensation in response to seasonal temperature change.

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Lactate dehydrogenase in abdominal muscle of crayfishOrconectes limosus and shrimpcrangon crangon (Decapoda: Crustacea): Properties and evolutionary relationship

Cited by 17 publications

References 23 publications

Effects of temperature acclimation on lactate dehydrogenase of cod(Gadus morhua): genetic, kinetic and thermodynamic aspects

Effects of temperature acclimation on lactate dehydrogenase of cod(Gadus morhua): genetic, kinetic and thermodynamic aspects

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Environmentally low-temperature kinetic and thermodynamic study of lactate dehydrogenase from Atlantic cod (G. morhua) using a 96-well microplate technique

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