Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium (Q27749365)

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U Gerike

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M J Danson

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D W Hough

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G L Taylor

A perspective on the biotechnological potential of extremophiles

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language of work or name

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15 March 1998

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published in

Structure

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volume

6

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issue

3

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page(s)

351-61

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Sequence and homology model of 3-isopropylmalate dehydrogenase from the psychrotrophic bacterium Vibrio sp. I5 suggest reasons for thermal instability

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Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 25 Angstroms Resolution

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Cold adaption of enzymes: structural comparison between salmon and bovine trypsins

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Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution

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Crystal structure of an open conformation of citrate synthase from chicken heart at 2.8-A resolution

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The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum

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The Crystal Structure of Citrate Synthase from the Hyperthermophilic Archaeon Pyrococcus furiosus at 1.9 Å Resolution,

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Sequencing and Expression of the Gene Encoding a Cold‐Active Citrate Synthase from an Antarctic Bacterium, Strain DS2‐3R

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Citrate synthase from the hyperthermophilic Archaeon, Pyrococcus furiosus

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Citrate synthase from the thermophilic archaebacterium Thermoplasma acidophilium. Cloning and sequencing of the gene

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Cold adaptation parameters derived from cDNA sequencing and molecular modelling of elastase from Antarctic fish Notothenia neglecta

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Design of fast enzymes by optimizing interaction potential in active site.

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Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability

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Comparative molecular dynamics simulation studies of salmon and bovine trypsins in aqueous solution

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Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin

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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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A reassessment of the molecular origin of cold denaturation

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

9551556

1 reference

Consolidated OpenCitations Corpus – April 2017