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Literature summary for 3.1.21.4 extracted from

  • Senejani, A.G.; Gogarten, J.P.
    Structural stability and endonuclease activity of a PI-SceI GFP-fusion protein (2007), Int. J. Biol. Sci., 3, 205-211.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escheichia coli, induction at 15°C results in accumulation in the cytoplasm, induction at 20-37°C results in formation of inclusion bodies Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information enzyme is an endonuclease encoded as a protein insert or intein within the yeast V-ATPase catalytic subunit encoding gene vma1. Insertion of the Green Fluorescence Protein into a loop which is located between the endonuclease and splicing domains of the Sce VMA1 intein. The GFP is functional and the additional GFP domain does not prevent intein excision and endonuclease activity. Contrary to wild-type, mutant requires the presence of Mn2+ and not Mg2+ ions for activity Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for wild-type activity Saccharomyces cerevisiae
Mn2+ required for activity of mutant which carries an insertion of the Green Fluorescence Protein into a loop which is located between the endonuclease and splicing domains of the Sce VMA1 intein Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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isoform SceI
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