Characterization of an extremely thermostable glutamate dehydrogenase: a key enzyme in the primary metabolism of the hyperthermophilic archaebacterium, Pyrococcus furiosus-Reference-Cited by-同舟云学术

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

Published:1992-04 Issue:3 Volume:1120 Page:267-272
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Robb Frank T.,Park Jae-Bum,Adams Michael W.W.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference34 articles.

1. Ultrathin mycelia-forming organisms from submarine volcanic areas having an optimum growth temperature of 105 °C

2. Hyperthermophilic microorganisms

3. Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100�C

4. Conversion of acetic acid to methane by thermophiles

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