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Structure of a hyperthermostable carbonic anhydrase identified from an active hydrothermal vent chimneyStructure of a hyperthermostable carbonic anhydrase identified from an active hydrothermal vent chimney
Structural highlights
Publication Abstract from PubMedCarbonic anhydrases (CAs) are extremely fast enzymes, which have attracted much interest in the past due to their medical relevance and their biotechnological potential. An alpha-type CA gene was isolated from DNA derived from an active hydrothermal vent chimney, in an effort to identify novel CAs with suitable properties for CO2 capture. The gene product was recombinantly produced and characterized, revealing remarkable thermostability, also in the presence of high ionic strength alkaline conditions, which are used in some CO2 capture applications. The Tm was above 90 degrees C under all tested conditions. The enzyme was crystallized and the structure determined by molecular replacement, revealing a typical bacterial alpha-type CA non-covalent dimer, but not the disulphide mediated tetramer observed for the hyperthermophilic homologue used for molecular replacement, from Thermovibrio ammonificans. Structural comparison suggests that an increased secondary structure content, increased content of charges on the surface and ionic interactions compared to mesophilic enzymes, may be main structural sources of thermostability, as previously suggested for the homologue from Sulfurihydrogenibium yellowstonense. Structure of a hyperthermostable carbonic anhydrase identified from an active hydrothermal vent chimney.,Fredslund F, Borchert MS, Poulsen JN, Mortensen SB, Perner M, Streit WR, Lo Leggio L Enzyme Microb Technol. 2018 Jul;114:48-54. doi: 10.1016/j.enzmictec.2018.03.009. , Epub 2018 Mar 30. PMID:29685353[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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