The crystal structure of an EST2 mutant unveils structural insights on the H group of the carboxylesterase/lipase family(1052 views) De Simone G, Menchise V, Alterio V, Mandrich L, Rossi M, Manco G, Pedone C
Keywords: Crystal Structure, Domain Swapping, Hsl, Lipase, Thermophilic Carboxylesterase, Dimer, Esterase Ii, Mutant Protein, Triacylglycerol Lipase, Unclassified Drug, Amino Terminal Sequence, Article, Crystallography, Enzyme Binding, Enzyme Mechanism, Enzyme Specificity, Enzyme Structure, Enzyme Substrate, Isomerization, Priority Journal, Protein Domain, Protein Family, Site Directed Mutagenesis, Structure Analysis, Three Dimensional Imaging, Amino Acid Sequence, Bacillus, Binding Sites, Chromatography, X-Ray, Dimerization, Enzyme Stability, Models, Molecular, Site-Directed, Mutation, Protein Conformation, Protein Engineering, Protein Structure, Secondary, Tertiary, Substrate Specificity, Temperature, Water, Alicyclobacillus, Alicyclobacillus Acidocaldarius,
Affiliations: *** IBB - CNR ***
Dipto. Chim. Biol.-Sezione B., University of Naples Federico II, Via Mezzocannone 16, 80134 N., Italy
Bioindustry Park del Canavese, Via Ribes 5, Colleretto Giocosa I-10010, Italy, Italy
Ist. di Biochim. Delle Proteine-CNR, Via P. Castellino 111, 80131 Naples, Italy, Italy
Dipto. Chim. Biol. -Sezione B., University of Naples Federico II, Via Mezzocannone 16, 80134 N., Italy
References: Not available.
The crystal structure of an EST2 mutant unveils structural insights on the H group of the carboxylesterase/lipase family