(Q27732563)

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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

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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 (English)

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Pyrococcus furiosus

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Pyrococcus furiosus

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author name string

K S Yip

1

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T J Stillman

2

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K L Britton

3

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P J Artymiuk

4

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P J Baker

5

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S E Sedelnikova

6

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P C Engel

7

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A Pasquo

8

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R Chiaraluce

9

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V Consalvi

10

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publication date

15 November 1995

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3

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1147-58

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11

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Life in hot springs and hydrothermal vents

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The chemistry of life at the margins

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Purification and properties of extremely thermostable glutamate dehydrogenases from two hyperthermophilic archaebacteria, Pyrococcus woesei and Pyrococcus furiosus

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Extremely thermostable glutamate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus furiosus

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Characterization of an extremely thermostable glutamate dehydrogenase: a key enzyme in the primary metabolism of the hyperthermophilic archaebacterium, Pyrococcus furiosus

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The protein sequence of glutamate dehydrogenase from Sulfolobus solfataricus, a thermoacidophilic archaebacterium. Is the presence of N-epsilon-methyllysine related to thermostability?

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The glutamate dehydrogenase-encoding gene of the hyperthermophilic archaeon Pyrococcus furiosus: sequence, transcription and analysis of the deduced amino acid sequence.

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The amino acid sequence of glutamate dehydrogenase from Pyrococcus furiosus, a hyperthermophilic archaebacterium

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Insights into thermal stability from a comparison of the glutamate dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis

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Subunit assembly and active site location in the structure of glutamate dehydrogenase

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Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis

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Structural relationship between the hexameric and tetrameric family of glutamate dehydrogenases

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Crystallization of the NAD(P)-dependent glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus.

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Crystallization of an NAD+-dependent glutamate dehydrogenase from Clostridium symbiosum

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Interior and surface of monomeric proteins

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Volume changes on protein folding.

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Ion-pairs in proteins.

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Strength and co-operativity of contributions of surface salt bridges to protein stability

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10.1016/S0969-2126(01)00251-9

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