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Table 1 Extremophilic enzymes studied for function in low water activity

From: Function and biotechnology of extremophilic enzymes in low water activity

Name Organism(s) Method(s) Reference(s)
Salt adapted
α-amylase Halothermothrix sp. CD spectroscopy, sedimentation velocity, crystal structure [59]
α-amylase Pseudoalteromonas sp. CD and fluorescence spectroscopy [53]
Carbonic anhydrase Dunaliella sp. Crystal structure [125]
Cysteinyl tRNA synthetase Halobacterium sp. Mutagenesis [126]
Dihydrofolate
reductase
Halobacterium sp. Homology modeling [127]
Dihydrofolate reductase Haloferax sp. Crystal structure [41]
Dihydrofolate reductase Haloarcula sp., Halobacterium sp., Haloquadratum sp., Natrosomonas sp. Homology modeling [38]
Dihydrolipoamide dehydrogenase Haloferax sp. Homology modeling, site-directed mutagenesis [50]
DNA ligase Haloferax sp. Mutagenesis [128]
DNA ligase Haloferax sp. Site-directed mutagenesis, CD, fluorescence and NMR spectroscopy [35]
DNA ligase Haloferax sp. Homology modeling, CD spectroscopy [26]
Esterase Haloarcula sp. Homology modeling, CD spectroscopy [43]
Ferredoxin [2Fe-2S] Haloarcula sp. Crystal structure [29]
Ferredoxin [2Fe-2S] Halobacterium sp. Fluorescence and CD spectroscopy [48, 129]
Glutamate dehydrogenase Halobacterium sp. Homology modeling [130]
Glucose dehydrogenase Haloferax sp. Crystal structure [30]
Glutaminase Micrococcus sp. Crystallization and X-ray crystallography [131]
Malate dehydrogenase Halobacterium sp. Fluorescence spectroscopy [132]
Malate dehydrogenase Halobacterium sp. Neutron scattering, ultracentrifugation and quasi-elastic light-scattering [46]
Malate dehydrogenase Haloarcula sp. Densitometry and neutron scattering [133]
Malate dehydrogenase Haloarcula sp. X-ray crystallography [28]
Malate dehydrogenase Haloarcula sp. Site-directed mutagenesis [134]
Malate dehydrogenase Haloarcula sp. Mutagenesis, crystal structure [135]
Malate dehydrogenase Haloarcula sp. Crystal structure, neutron scattering [23]
Malate dehydrogenase Salinibacter sp. Analytical centrifugation, CD spectroscopy [136]
Malate dehydrogenase Haloarcula sp. Neutron diffraction, CD and neutron spectroscopy [19]
Malate dehydrogenase Haloarcula sp. Neutron spectroscopy [137]
Nucleoside diphosphate kinase Haloarcula sp. CD spectroscopy, crystal structure [52]
Proliferating cell nuclear antigen Haloferax sp. Crystal structure [42]
Protease Halobacillus sp. Fluorescence resonance energy transfer [51]
TATA-box binding protein Pyrococcus sp. Analytical ultracentrifugation, isothermal titration calorimetry [54]
TATA-box binding protein Pyrococcus sp. Site-directed mutagenesis, isothermal titration calorimetry [5557]
Xylanase Bacillus sp. Crystal structure [138]
Cold active
Adenylate kinase Bacillus sp. Crystal structure [85]
Adenylate kinase Marinibacillus sp. Crystal structure, CD spectroscopy [139]
Alkaline phosphatase Gadus sp. Fluorescence spectroscopy [140]
Alkaline phosphatase Antarctic strain TAB5 Site-directed mutagenesis [84, 141]
Alkaline phosphatase Vibrio sp. Mutagenesis, CD spectroscopy [142]
Aminopeptidase Colwellia sp. Crystal structure [143]
Aminopeptidase Colwellia sp. Differential scanning calorimetry, fluorescence spectroscopy [144]
α-amylase Alteromonas sp. Crystal structure [86]
α-amylase Pseudoalteromonas sp. Mutagenesis, differential scanning calorimetry, fluorescence spectroscopy [145]
α-amylase Pseudoalteromonas sp. Differential scanning calorimetry, fluorescence spectroscopy [79]
α-amylase Pseudoalteromonas sp. Matrix assisted laser desorption ionization time-of-flight mass spectrometry [146]
α-amylase Alteromonas sp. Mutagenesis, crystal structure, molecular dynamics simulations [147]
Aspartate aminotransferase Pseudoalteromonas sp. Homology modeling, CD and fluorescence spectroscopy [148]
β-galactosidase Arthrobacter sp. Crystal structure [149]
β-lactamase Pseudomonas sp. Crystal structure [87]
Catalase Vibrio sp. Differential scanning calorimetry, fluorescence spectroscopy [150]
Catalase Vibrio sp. Crystal structure [151]
Chitinase Arthrobacter sp. Homology-modeling, mutagenesis, fluorescence spectroscopy [77]
Chitobiase Arthrobacter sp. Differential scanning calorimetry [152]
Citrate synthase Antarctic bacterium DS2-3R Crystal structure [153]
Citrate synthase Arthrobacter sp. Site-directed mutagenesis [154]
Citrate synthase Sulfolobus sp. Crystal structure [155]
Citrate synthase Arthobacter sp., Pyrococcus sp. Homology modeling [156]
Endonuclease I Vibrio sp. Crystal structure [59]
Esterase Pseudoalteromonas sp. Fourier transform infrared spectroscopy, molecular dynamics simulation [78]
Iron superoxide Pseudoalteromonas sp. Crystal structure, CD and fluorescence spectroscopy [75]
Lipase Photobacterium sp. Crystal structure [157]
Malate dehydrogenase Aquaspirillium sp. Crystal structure [88]
Nitrate reductase Shewanella sp. Homology modeling [158]
Pepsin Trematomus sp. Homology modeling [159]
Protease Bacillus sp. Homology modeling, mutagenesis, CD spectroscopy [160]
Protease Pseudomonas sp. Crystal structure [161]
Protease Pseudoalteromonas sp. Homology modeling, CD, fluorescence spectroscopy [162]
Protease Bacillus sp. Homology modeling, mutagenesis [163]
Protease Vibrio sp. Site-directed mutagenesis [164]
Protease Bacillus sp. Crystal structure [165]
Protease Geomicrobium sp. Homology modeling, CD and fluorescence spectroscopy [166, 167]
Ribonuclease Shewanella sp. Site-directed mutagenesis, CD spectroscopy [168]
Superoxide dismutase Aliivibrio sp. Crystal structure, differential scanning calorimetry [93]
Subtilisin Bacillus sp. Site-directed mutagenesis [169]
Triose phosphate isomerase Vibrio sp. Crystal structures, calorimetry [98]
Organic solvent active
Alcohol dehydrogenase Rhodococcus sp. Crystal structure [119]
Protease Pseudomonas sp. Site-directed and random mutagenesis [116, 117]
Protease Pseudomonas sp. Homology modeling [118]