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Structure and Stability of the Dimeric Triosephosphate Isomerase from the Thermophilic Archaeon Ther...

Structure and Stability of the Dimeric Triosephosphate Isomerase from the Thermophilic Archaeon Ther...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1752179614

Structure and Stability of the Dimeric Triosephosphate Isomerase from the Thermophilic Archaeon Thermoplasma acidophilum

About this item

Full title

Structure and Stability of the Dimeric Triosephosphate Isomerase from the Thermophilic Archaeon Thermoplasma acidophilum

Publisher

United States: Public Library of Science

Journal title

PloS one, 2015-12, Vol.10 (12), p.e0145331-e0145331

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

Thermoplasma acidophilum is a thermophilic archaeon that uses both non-phosphorylative Entner-Doudoroff (ED) pathway and Embden-Meyerhof-Parnas (EMP) pathway for glucose degradation. While triosephosphate isomerase (TPI), a well-known glycolytic enzyme, is not involved in the ED pathway in T. acidophilum, it has been considered to play an important...

Alternative Titles

Full title

Structure and Stability of the Dimeric Triosephosphate Isomerase from the Thermophilic Archaeon Thermoplasma acidophilum

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1752179614

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1752179614

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0145331

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