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Evolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon.

Extremophilic organisms require specialized enzymes for their exotic metabolisms. Acid-loving thermophilic Archaea that live in the mudpots of volcanic solfataras obtain their energy from reduced sulphur compounds such as hydrogen sulphide ([H.sub.2]S) and carbon disulphide (C[S.sub.2]) (1,2). The o... Full description

Journal Title: Nature October 19, 2011, Vol.478(7369), pp.412-416
Main Author: Smeulders, Marjan J
Other Authors: Barends, Thomas R M , Pol, Arjan , Scherer, Anna , Zandvoort, Marcel H , Udvarhelyi, Anikó , Khadem, Ahmad F , Menzel, Andreas , Hermans, John , Shoeman, Robert L , Wessels, Hans J C T , van Den Heuvel, Lambert P , Russ, Lina , Schlichting, Ilme , Jetten, Mike S M , Op Den Camp, Huub J M
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1476-4687 ; DOI: 10.1038/nature10464
Link: http://search.proquest.com/docview/900626515/?pq-origsite=primo
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title: Evolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon.
format: Article
creator:
  • Smeulders, Marjan J
  • Barends, Thomas R M
  • Pol, Arjan
  • Scherer, Anna
  • Zandvoort, Marcel H
  • Udvarhelyi, Anikó
  • Khadem, Ahmad F
  • Menzel, Andreas
  • Hermans, John
  • Shoeman, Robert L
  • Wessels, Hans J C T
  • van Den Heuvel, Lambert P
  • Russ, Lina
  • Schlichting, Ilme
  • Jetten, Mike S M
  • Op Den Camp, Huub J M
subjects:
  • Acidianus–Classification
  • Carbon Disulfide–Enzymology
  • Catalytic Domain–Genetics
  • Crystallography, X-Ray–Metabolism
  • Evolution, Molecular–Chemistry
  • Hydrolases–Genetics
  • Models, Molecular–Genetics
  • Molecular Sequence Data–Genetics
  • Mutation–Genetics
  • Phylogeny–Genetics
  • Protein Structure, Tertiary–Genetics
  • Hydrolases
  • Carbon Disulfide
ispartof: Nature, October 19, 2011, Vol.478(7369), pp.412-416
description: Extremophilic organisms require specialized enzymes for their exotic metabolisms. Acid-loving thermophilic Archaea that live in the mudpots of volcanic solfataras obtain their energy from reduced sulphur compounds such as hydrogen sulphide ([H.sub.2]S) and carbon disulphide (C[S.sub.2]) (1,2). The oxidation of these compounds into sulphuric acid creates the extremely acidic environment that characterizes solfataras. The hyperthermophilic Acidianus strain A1-3, which was isolated from the fumarolic, ancient sauna building at the Solfatara volcano (Naples, Italy), was shown to rapidly convert C[S.sub.2] into [H.sub.2]S and carbon dioxide (C[O.sub.2]), but nothing has been known about the modes of action and the evolution of the enzyme(s) involved. Here we describe the structure, the proposed mechanism and evolution of a C[S.sub.2] hydrolase from Acidianus A1-3. The enzyme monomer displays a typical [beta]-carbonic anhydrase fold and active site, yet C[O.sub.2] is not one of its substrates. Owing to large carboxy- and amino-terminal arms, an unusual hexadecameric catenane oligomer has evolved. This structure results in the blocking of the entrance to the active site that is found in canonical [beta]-carbonic anhydrases and the formation of a single 15-[Angstrom]-long, highly hydrophobic tunnel that functions as a specificity filter. The tunnel determines the enzyme's substrate specificity for C[S.sub.2], which is hydrophobic. The transposon sequences that surround the gene encoding this C[S.sub.2] hydrolase point to horizontal gene transfer as a mechanism for its acquisition during evolution. Our results show how the ancient [beta]-carbonic anhydrase, which is central to global carbon metabolism, was transformed by divergent evolution into a crucial enzyme in C[S.sub.2] metabolism.
language: eng
source:
identifier: E-ISSN: 1476-4687 ; DOI: 10.1038/nature10464
fulltext: fulltext
issn:
  • 14764687
  • 1476-4687
url: Link


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titleEvolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon.
creatorSmeulders, Marjan J ; Barends, Thomas R M ; Pol, Arjan ; Scherer, Anna ; Zandvoort, Marcel H ; Udvarhelyi, Anikó ; Khadem, Ahmad F ; Menzel, Andreas ; Hermans, John ; Shoeman, Robert L ; Wessels, Hans J C T ; van Den Heuvel, Lambert P ; Russ, Lina ; Schlichting, Ilme ; Jetten, Mike S M ; Op Den Camp, Huub J M
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ispartofNature, October 19, 2011, Vol.478(7369), pp.412-416
identifierE-ISSN: 1476-4687 ; DOI: 10.1038/nature10464
subjectAcidianus–Classification ; Carbon Disulfide–Enzymology ; Catalytic Domain–Genetics ; Crystallography, X-Ray–Metabolism ; Evolution, Molecular–Chemistry ; Hydrolases–Genetics ; Models, Molecular–Genetics ; Molecular Sequence Data–Genetics ; Mutation–Genetics ; Phylogeny–Genetics ; Protein Structure, Tertiary–Genetics ; Hydrolases ; Carbon Disulfide
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descriptionExtremophilic organisms require specialized enzymes for their exotic metabolisms. Acid-loving thermophilic Archaea that live in the mudpots of volcanic solfataras obtain their energy from reduced sulphur compounds such as hydrogen sulphide ([H.sub.2]S) and carbon disulphide (C[S.sub.2]) (1,2). The oxidation of these compounds into sulphuric acid creates the extremely acidic environment that characterizes solfataras. The hyperthermophilic Acidianus strain A1-3, which was isolated from the fumarolic, ancient sauna building at the Solfatara volcano (Naples, Italy), was shown to rapidly convert C[S.sub.2] into [H.sub.2]S and carbon dioxide (C[O.sub.2]), but nothing has been known about the modes of action and the evolution of the enzyme(s) involved. Here we describe the structure, the proposed mechanism and evolution of a C[S.sub.2] hydrolase from Acidianus A1-3. The enzyme monomer displays a typical [beta]-carbonic anhydrase fold and active site, yet C[O.sub.2] is not one of its substrates. Owing to large carboxy- and amino-terminal arms, an unusual hexadecameric catenane oligomer has evolved. This structure results in the blocking of the entrance to the active site that is found in canonical [beta]-carbonic anhydrases and the formation of a single 15-[Angstrom]-long, highly hydrophobic tunnel that functions as a specificity filter. The tunnel determines the enzyme's substrate specificity for C[S.sub.2], which is hydrophobic. The transposon sequences that surround the gene encoding this C[S.sub.2] hydrolase point to horizontal gene transfer as a mechanism for its acquisition during evolution. Our results show how the ancient [beta]-carbonic anhydrase, which is central to global carbon metabolism, was transformed by divergent evolution into a crucial enzyme in C[S.sub.2] metabolism.
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titleEvolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon.
authorSmeulders, Marjan J ; Barends, Thomas R M ; Pol, Arjan ; Scherer, Anna ; Zandvoort, Marcel H ; Udvarhelyi, Anikó ; Khadem, Ahmad F ; Menzel, Andreas ; Hermans, John ; Shoeman, Robert L ; Wessels, Hans J C T ; van Den Heuvel, Lambert P ; Russ, Lina ; Schlichting, Ilme ; Jetten, Mike S M ; Op Den Camp,...
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