The structure of a tetrameric α-carbonic anhydrase from Thermovibrio ammonificans reveals a core formed around intermolecular disulfides that contribute to its thermostability

Acta Crystallographica Section D: Biological Crystallography

Volumn 70, Issue 10, 2014, Pages 2607-2618

  James, Paul ^a   Isupov, Michail N ^a   Sayer, Christopher ^a   Saneei, Vahid ^a   Berg, Svein ^b   Lioliou, Maria ^b   Kotlar, Hans Kristian ^b   Littlechild, Jennifer A ^a  

^a UNIVERSITY OF EXETER   (United Kingdom)

^b STATOIL   (Norway)

Author keywords

acetazolamide; carbon dioxide capture; carbonic anhydrase; thermal stability; thermophilic

Indexed keywords

4-NITROPHENYL ACETATE; ACETAZOLAMIDE; BACTERIAL PROTEIN; CARBON DIOXIDE; CARBONATE DEHYDRATASE; CARBONATE DEHYDRATASE INHIBITOR; DISULFIDE; NITROPHENOL; SULFANILAMIDE; SULFANILAMIDE DERIVATIVE;

BACTERIUM; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME STABILITY; GENETICS; KINETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR MODEL; PROTEIN CONFORMATION; TEMPERATURE; X RAY CRYSTALLOGRAPHY;

ACETAZOLAMIDE; BACTERIA; BACTERIAL PROTEINS; CARBON DIOXIDE; CARBONIC ANHYDRASE INHIBITORS; CARBONIC ANHYDRASES; CATALYTIC DOMAIN; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; DISULFIDES; ENZYME STABILITY; KINETICS; MODELS, MOLECULAR; NITROPHENOLS; PROTEIN CONFORMATION; SULFANILAMIDES; TEMPERATURE;

EID: 84907855953     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S1399004714016526     Document Type: Article

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