A highly acid-stable and thermostable endo-beta-glucanase from the thermoacidophilic archaeon Sulfolobus solfataricus.
Huang
Yiwei
Y
Institute of Biochemistry, University of Bayreuth, Universitätstrasse 30, 95447 Bayreuth, Germany.
Krauss
Gerhard
G
Cottaz
Sylvain
S
Driguez
Hugues
H
Lipps
Georg
G
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry; D002480:Cellulase / Q000737:chemistry* / Q000378:metabolism; D004795:Enzyme Stability; D005656:Fungal Proteins / Q000737:chemistry; D006026:Glycoside Hydrolases / Q000378:metabolism; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D045245:Rhodothermus / Q000201:enzymology; D016415:Sequence Alignment / Q000379:methods; D020539:Sequence Analysis, Protein / Q000379:methods; D048170:Streptomyces lividans / Q000201:enzymology; D048229:Sulfolobus solfataricus / Q000201:enzymology*; D014242:Trichoderma / Q000201:enzymology
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D005656:Fungal Proteins; D006026:Glycoside Hydrolases; D002480:Cellulase; C090774:endoglucanase EGL1