A Temperature-dependent Conformational Change in d-Amino Acid Oxidase and Its Effect on Catalysis

Massey, Vincent; Curti, Bruno; Ganther, Howard E.

doi:10.1016/s0021-9258(18)96628-7

Cited by 248 publications

(76 citation statements)

References 26 publications

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“…We earlier interpreted our data as a reversible denaturat,ion of the enzyme (1). With the modifiers, Levy et al (11) and Azuma and Tonomura (16) argued for a temperature-dependent conformation change, as is also suggested for some other enzymes with biphasic Arrhenius plots (19)(20)(21). Possible schemes for the action of modifiers on myosin have been proposed (16,18,22).…”

Section: Discussionsupporting

confidence: 63%

Hydrostatic pressure effects on rabbit and echinoderm myosin ATPase

Guthe

1969

Archives of Biochemistry and Biophysics

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When saturated with ATP, sea cucumber myosin hydrolyzes ATP about 15 times more slowly than rabbit myosin, as expected from the slower contraction time of the muscle. The Arrhenius plots coincide at low temperatures, but only the rabbit plot changes slope at higher temperatures. This unexpected change in slope apparently results from the use of Verona1 buffer. At high substrate concentrations in Verona1 buffer, the enzymatic activities of the two proteins depend identically on calcium ion and on pH. The two myosins are equally inhibited by pressure at low pH and activated at high, suggesting that structural features common to the two enzymes are responsible for pressure sensitivity and its pH dependence.

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Section: Discussionsupporting

confidence: 63%

Hydrostatic pressure effects on rabbit and echinoderm myosin ATPase

Guthe

1969

Archives of Biochemistry and Biophysics

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“…The situation is somewhat analogous to the classic example of D-amino acid oxidase, whose tryptophan fluorescence decreases according to a sigmoidlike curve on raising the temperature (28). This phenomenon was first attributed to a conformational change (28) but later shown to be a consequence of dynamic quenching (29). To decide whether the change we observed could be due to a temperature-induced two-state conformational transition, we carried out CD, DSC, and ITC measurements.…”

Section: Conformational Transition or A Change In Conformational Fluctuations?mentioning

confidence: 64%

“…However, because IPM binding is likely to be also affected by the conformational fluctuations (especially the relative domain-domain motions), it may also reflect a change in the amplitude or mode of these fluctuations. The situation is somewhat analogous to the classic example of D-amino acid oxidase, whose tryptophan fluorescence decreases according to a sigmoidlike curve on raising the temperature (28). This phenomenon was first attributed to a conformational change (28) but later shown to be a consequence of dynamic quenching (29).…”

Section: Conformational Transition or A Change In Conformational Fluctuations?mentioning

confidence: 68%

A Link between Hinge-Bending Domain Motions and the Temperature Dependence of Catalysis in 3-Isopropylmalate Dehydrogenase

Hajdú

Szilágyi

Kardos

et al. 2009

Biophysical Journal

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Enzyme function depends on specific conformational motions. We show that the temperature dependence of enzyme kinetic parameters can provide insight into these functionally relevant motions. While investigating the catalytic properties of IPMDH from Escherichia coli, we found that its catalytic efficiency (k(cat)/K(M,IPM)) for the substrate IPM has an unusual temperature dependence, showing a local minimum at approximately 35 degrees C. In search of an explanation, we measured the individual constants k(cat) and K(M,IPM) as a function of temperature, and found that the van 't Hoff plot of K(M,IPM) shows sigmoid-like transition in the 20-40 degrees C temperature range. By means of various measurements including hydrogen-deuterium exchange and fluorescence resonance energy transfer, we showed that the conformational fluctuations, including hinge-bending domain motions increase more steeply with temperatures >30 degrees C. The thermodynamic parameters of ligand binding determined by isothermal titration calorimetry as a function of temperature were found to be strongly correlated to the conformational fluctuations of the enzyme. Because the binding of IPM is associated with a hinge-bending domain closure, the more intense hinge-bending fluctuations at higher temperatures increasingly interfere with IPM binding, thereby abruptly increasing its dissociation constant and leading to the observed unusual temperature dependence of the catalytic efficiency.

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“…Hence, reasons for convexity might more likely be attributed to the presence of competing enzymatic forms or multiple coexisting enzymes, each dominating at a specific temperature range 43 , and/or displaying different kinetics under different temperatures. In addition, possible temperature-induced variations in the composition of a system microbial community cannot be underestimated, as this could also influence the presence and/or abundance of certain enzymes in the system.…”

Section: Resultsmentioning

confidence: 99%

Understanding the Dependence of Micropollutant Biotransformation Rates on Short-Term Temperature Shifts

Meynet

Davenport

Fenner

2020

Environ. Sci. Technol.

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Temperature is a key factor that influences chemical biotransformation potential and rates, on which exposure and fate models rely to predict the environmental (micro)pollutant fate. Arrhenius-based models are currently implemented in environmental exposure assessment to adapt biotransformation rates to actual temperatures, assuming validity in the 0-30 °C range. However, evidence on how temperature shifts affect the physicochemical and microbial features in biological systems is scarce, questioning the validity of the existing modeling approaches. In this work, laboratory-scale batch assays were designed to investigate how a mixed microbial community responds to short-term temperature shifts, and how this impacts its ability to biotransform a range of structurally diverse micropollutants. Our results revealed three distinct kinetic responses at temperatures above 20 °C, mostly deviating from the classic Arrheniustype behavior. Micropollutants with similar temperature responses appeared to undergo mostly similar initial biotransformation reactions, with substitution-type reactions maintaining Arrhenius-type behavior up to higher temperatures than oxidation-type reactions. Above 20 °C, the microbial community also showed marked shifts in both composition and activity, which mostly correlated with the observed deviations from Arrhenius-type behavior, with compositional changes becoming a more relevant factor in biotransformations catalyzed by more specific enzymes (e.g., oxidation reactions). Our findings underline the need to re-examine and further develop current environmental fate models by integrating biological aspects, to improve accuracy in predicting the environmental fate of micropollutants.

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A Temperature-dependent Conformational Change in d-Amino Acid Oxidase and Its Effect on Catalysis

Cited by 248 publications

References 26 publications

Hydrostatic pressure effects on rabbit and echinoderm myosin ATPase

Hydrostatic pressure effects on rabbit and echinoderm myosin ATPase

A Link between Hinge-Bending Domain Motions and the Temperature Dependence of Catalysis in 3-Isopropylmalate Dehydrogenase

Understanding the Dependence of Micropollutant Biotransformation Rates on Short-Term Temperature Shifts

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