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Literature summary extracted from

  • Giordano, A.; Russo, C.; Raia, C.A.; Kuznetsova, I.M.; Stepanenko, O.V.; Turoverov, K.K.
    Highly UV-absorbing complex in selenomethionine-substituted alcohol dehydrogenase from Sulfolobus solfataricus (2004), J. Proteome Res., 3, 613-620.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.1 selenium the effect of significant decrease in intrinsic fluorescence intensity of the enzyme caused by replacement of S atoms of methionine residues to Se is explained on the basis of the analysis of its 3D structure. All selenium atoms are located far from both Trp95 and Trp117 and can not cause their fluorescence quenching. Substitution of S by Se causes enhanced protein absorption in the UV-region. This effect is explained by the formation of Se complex with some groups of protein Saccharolobus solfataricus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.1 Saccharolobus solfataricus P39462
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.1
-
Saccharolobus solfataricus

Synonyms

EC Number Synonyms Comment Organism
1.1.1.1 SSADH
-
Saccharolobus solfataricus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.1 NAD+
-
Saccharolobus solfataricus