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Literature summary for 2.5.1.81 extracted from

  • Lee, P.C.; Mijts, B.N.; Petri, R.; Watts, K.T.; Schmidt-Dannert, C.
    Alteration of product specificity of Aeropyrum pernix farnesylgeranyl diphosphate synthase (Fgs) by directed evolution (2004), Protein Eng. Des. Sel., 17, 771-777.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli Aeropyrum pernix

Protein Variants

Protein Variants Comment Organism
additional information directed evolution is used to create mutant FGPP synthases that confirm the importance of amino acids upstream of the FARM of prenyl diphosphate synthases and demonstrate the significance of mutations upstream of an additional conserved region (141GQ142). Product chain-length distribution can be also controlled by a structural change provoked by a cooperative interaction of amino acids Aeropyrum pernix

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix Q9UWR6
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Purification (Commentary)

Purification (Comment) Organism
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Aeropyrum pernix

Synonyms

Synonyms Comment Organism
C25 FGPP synthase
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Aeropyrum pernix
farnesylgeranyl diphosphate synthase
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Fgs
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Aeropyrum pernix