Function and biotechnology of extremophilic enzymes in low water activity

Karan, Ram; Capes, Melinda D; DasSarma, Shiladitya

doi:10.1186/2046-9063-8-4

Aquatic Biosystems

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	[55–57]
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]

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