The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures

Yip, Kitty S. P.; Stillman, Timothy J.; Britton, K.L.; Artymiuk, Peter J.; Baker, Patrick J.; Sedelnikova, Svetlana E.; Engel, Paul C.; Pasquo, Alessandra; Chiaraluce, Roberta; Consalvi, Valerio; Scandurra, Roberto; Rice, David W.

doi:10.1016/s0969-2126(01)00251-9

Cited by 435 publications

(365 citation statements)

References 54 publications

(79 reference statements)

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“…The observation that especially the subunit contacts are intensified by a strikin! ; increase in ion pairs (as found for the malate dehydrogenas,," from Thermusflavus [6] and the glutamate dehydrogenase fr~,m Pyrococcusfuriosus [5]) and hydrophobic interactions (as reported for the glyceraldehyde-3-phosphate dehydrogenase fr~,m Thermotoga maritima [4]) suggests that the subunit con-*(orresponding author. Fax: (49) (201) 183 2529.…”

Section: Introductionmentioning

confidence: 76%

“…From the suggested importance of the intersubunit contacts for thermostabilization, as deduced from experimental and comparative studies on various oligomeric enzymes [4][5][6][7], one should expect that the benefit of the higher association state resides in an increase of protein thermostability. The observation that the preference of a higher association state does not generally apply (or even countercurrent trends occur, as shown in the case of the enolases [25]) indicates that the advantage of association is limited by functional and/or structural restraints.…”

Section: Molecular Mass Determinationsmentioning

confidence: 99%

“…From the various studies different featu,'es have been discussed as responsible for the increased conformational stability at all three levels of protein structure (c~,re region and secondary structure elements, interactions between domains and subunits): e.g. reduction of solvent acce~sible area and increase in the fraction of buried atoms [1], st~bilization of a-helices, strengthening of polypeptide chain teTmini and loops [2], shortening of loops [3], increase of ion bridges and hydrophobic interactions [4][5][6]. The observation that especially the subunit contacts are intensified by a strikin!…”

Section: Introductionmentioning

confidence: 99%

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Tetrameric triosephosphate isomerase from hyperthermophilic Archaea

1996

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Section: Introductionmentioning

confidence: 76%

Section: Molecular Mass Determinationsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Tetrameric triosephosphate isomerase from hyperthermophilic Archaea

1996

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“…Indeed, the charge resonance of the guanidinium group gives arginine the possibility to form more than one salt bridge. For instance, Arg-mediated networks of ion pairs appear to be responsible for the unusual stability of glutamate dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus [66]. In addition, the arginine side chain can form up to five H-bonds, preferably to carbonyl oxygens [67].…”

Section: Structural Factors Affecting the Stability Of Psychrophilic mentioning

confidence: 99%

Psychrophilic enzymes: molecular basis of cold adaptation

Feller

Gerday

1997

CMLS, Cell. mol. life sci.

371

233

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Abstract. Psychrophilic organisms have successfully provides enhanced abilities to undergo conformational colonized polar and alpine regions and are able to grow changes during catalysis. Thermal instability of coldefficiently at sub-zero temperatures. At the enzymatic adapted enzymes is therefore regarded as a consequence level, such organisms have to cope with the reduction of of their conformational flexibility. A survey of the psychrophilic enzymes studied so far reveals only minor chemical reaction rates induced by low temperatures in alterations of the primary structure when compared to order to maintain adequate metabolic fluxes. Thermal compensation in cold-adapted enzymes is reached mesophilic or thermophilic homologues. However, all known structural factors and weak interactions inthrough improved turnover number and catalytic effivolved in protein stability are either reduced in number ciency. This optimization of the catalytic parameters can originate from a highly flexible structure which or modified in order to increase their flexibility.Key words. Psychrophiles; extremophiles; cold adaptation; microbial proteins; protein stability; weak interactions; Antarctic.Psychrophiles live at the lowest temperatures which allow the development of living organisms. These extremophilic organisms, either prokaryotic or eukaryotic, represent a major class of the living world if we consider the vast extent of permanently cold environments on Earth, such as polar and alpine regions or deep-sea waters. The successful colonization of such severe ecological niches by psychrophiles, their diversity and abundance are now well recognized. The lower temperature limit of life is commonly defined as the freezing point of cellular water. Although apparently simple by definition, this limit can drop significantly below 0°C, the freezing point of pure water. For instance, the freezing point of a typical marine teleost ranges between −0.5 and −0.9°C. Sodium chloride is responsible for about 85% of the freezing point depression, and the remaining 15% is due to other small solutes. Synthesis of antifreeze glycoproteins and peptides can further depress the freezing point of body fluids or cellular water. These proteins lower the freezing point by a noncolligative mechanism without altering the melting point significantly, and are therefore also referred to as thermal hysteresis proteins [1,2]. They were first discovered in the blood sera of Antarctic fish living perennially at about −1.9°C, but have been now reported in many organisms including plants, insects, fungi and bacteria [3][4][5]. Levels of thermal hysteresis activity generally range from 0.1 to 0.3°C in bacteria, from 0.2 to 0.5°C in plants, from 0.7 to 1.5°C in fish and from 3 to 6°C in insects. Besides the synthesis of cryoprotectants which lead to freeze avoidance, several organisms have developed mechanisms of freeze tolerance, involving drastic metabolic modifica-* Corresponding author.

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“…Mammalian GDH is ccxnposed of six identical subunits, and the regulation of GDH is very complex (Fisher, 1985). It is only in recent years that the three-dimensional structure of GDH from microorganisms has been available (Baker et al, 1992;Yip et al, 1995). There is, however, relatively low identity between the microbial and mammalian GDHs.…”

mentioning

confidence: 99%

Different Antigenic Reactivities of Bovine Brain Glutamate Dehydrogenase Isoproteins

Choi

Hong

Song

et al. 1999

Journal of Neurochemistry

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Abstract:The structural differences between two types of glutamate dehydrogenase (GDH) isoproteins (GDH I and GDH II), homogeneously isolated from bovine brain, were investigated using a biosensor technology and monoclonal antibodies. A total of seven monoclonal antibodies raised against GDH II were produced, and the antibodies recognized a single protein band that comigrates with purified GDH II on sodium dodecyl sulfatepolyacrylamide gel electrophoresis and immunoblot. Of seven anti-GDH II monoclonal antibodies tested in the immunoblot analysis, all seven antibodies interacted with GDH II, whereas only four antibodies recognized the protein band of the other GDH isoprotein, GDH 1. When inhibition tests of the GDH isoproteins were performed with the seven anti-GDH II monoclonal antibodies, three antibodies inhibited GDH II activity, whereas only one antibody inhibited GDH I activity. The binding affinity of anti-GDH II monoclonal antibodies for GDH II (K, = 1.0 nM) determined using a biosensor technology (Pharmacia BIAcore) was fivefold higher than for GDH I (K, = 5.3 nM). These results, together with epitope mapping analysis, suggest that there may be structural differences between the two GDH isoproteins, in addition to their different biochemical properties. Using the anti-GDH II antibodies as probes, we also investigated the crossreactivities of brain GDHs from some mammalian and an avian species, showing that the mammalian brain GDH enzymes are related immunologically to each other. Key Words: Glutamate dehydrogenase isoproteins-Monoclonal antibodies-Protein-protein interaction.

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The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures

Cited by 435 publications

References 54 publications

Tetrameric triosephosphate isomerase from hyperthermophilic Archaea

Tetrameric triosephosphate isomerase from hyperthermophilic Archaea

Psychrophilic enzymes: molecular basis of cold adaptation

Different Antigenic Reactivities of Bovine Brain Glutamate Dehydrogenase Isoproteins

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