Structure of a hyperthermostable carbonic anhydrase identified from an active hydrothermal vent chimney.

Fredslund, Folmer, Borchert, Martin S., Poulsen, Jens-Christian N., Mortensen, Steen Bennike, Perner, Mirjam , Streit, Wolfgang R. and Lo Leggio, Leila (2018) Structure of a hyperthermostable carbonic anhydrase identified from an active hydrothermal vent chimney. Enzyme and Microbial Technology, 114 . pp. 48-54. DOI 10.1016/j.enzmictec.2018.03.009.

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Supplementary data:

Abstract

Highlights

• A carbonic anhydrase gene was identified from an hydrothermal vent metagenome.
• The gene product LOGACA is a dimeric α-type carbonic anhydrase.
• LOGACA is highly thermostable at alkaline pH.
• Thermostability correlates with secondary structure, surface charges and ion pairs.

Abstract

Carbonic anhydrases (CAs) are extremely fast enzymes, which have attracted much interest in the past due to their medical relevance and their biotechnological potential. An α-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 °C under all tested conditions. The enzyme was crystallized and the structure determined by molecular replacement, revealing a typical bacterial α-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.

Document Type: Article
Keywords: Carbonic anhydrase, Thermostability, Metagenomics, Crystal structure
Research affiliation: OceanRep > GEOMAR > FB2 Marine Biogeochemistry > FB2-MG Marine Geosystems
Refereed: Yes
Open Access Journal?: No
DOI etc.: 10.1016/j.enzmictec.2018.03.009
ISSN: 0141-0229
Projects: SPP 1144 "From Mantle to Ocean"
Expeditions/Models/Experiments:
Date Deposited: 18 Jun 2018 11:00
Last Modified: 01 Feb 2019 15:02
URI: http://oceanrep.geomar.de/id/eprint/43432

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