Cristin-resultat-ID: 1897270
Sist endret: 2. desember 2021, 14:15
NVI-rapporteringsår: 2021
Resultat
Vitenskapelig artikkel
2021

Overview of structurally homologous flavoprotein oxidoreductases containing the low Mr thioredoxin reductase-like fold – A functionally diverse group

Bidragsytere:
  • Marta Hammerstad og
  • Hans-Petter Hersleth

Tidsskrift

Archives of Biochemistry and Biophysics
ISSN 0003-9861
e-ISSN 1096-0384
NVI-nivå 1

Om resultatet

Vitenskapelig artikkel
Publiseringsår: 2021
Publisert online: 2021
Trykket: 2021
Volum: 702
Sider: 1 - 19
Artikkelnummer: 108826
Open Access

Importkilder

Scopus-ID: 2-s2.0-85102303189

Klassifisering

Vitenskapsdisipliner

Biokjemi

Emneord

Strukturbiologi • Biokjemi • Enzymologi

Beskrivelse Beskrivelse

Tittel

Overview of structurally homologous flavoprotein oxidoreductases containing the low Mr thioredoxin reductase-like fold – A functionally diverse group

Sammendrag

Structural studies show that enzymes have a limited number of unique folds, although structurally related enzymes have evolved to perform a large variety of functions. In this review, we have focused on enzymes containing the low molecular weight thioredoxin reductase (low Mr TrxR) fold. This fold consists of two domains, both containing a three-layer ββα sandwich Rossmann-like fold, serving as flavin adenine dinucleotide (FAD) and, in most cases, pyridine nucleotide (NAD(P)H) binding-domains. Based on a search of the Protein Data Bank for all published structures containing the low Mr TrxR-like fold, we here present a comprehensive overview of enzymes with this structural architecture. These range from TrxR-like ferredoxin/flavodoxin NAD(P)+ oxidoreductases, through glutathione reductase, to NADH peroxidase. Some enzymes are solely composed of the low Mr TrxR-like fold, while others contain one or two additional domains. In this review, we give a detailed description of selected enzymes containing only the low Mr TrxR-like fold, however, catalyzing a diversity of chemical reactions. Our overview of this structurally similar, yet functionally distinct group of flavoprotein oxidoreductases highlights the fascinating and increasing number of studies describing the diversity among these enzymes, especially during the last decade(s).

Bidragsytere

Marta Hammerstad

  • Tilknyttet:
    Forfatter
    ved Seksjon for biokjemi og molekylærbiologi ved Universitetet i Oslo

Hans-Petter Hersleth

  • Tilknyttet:
    Forfatter
    ved Seksjon for biokjemi og molekylærbiologi ved Universitetet i Oslo
  • Tilknyttet:
    Forfatter
    ved Seksjon for kjemisk livsvitenskap - biomolekyler, bio-inspirerte materialer og bioanalytisk kjemi ved Universitetet i Oslo
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