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Literature summary extracted from

  • Dang, T.; Prestwich, G.D.
    Site-directed mutagenesis of squalene-hopene cyclase: altered substrate specificity and product distribution (2000), Chem. Biol., 7, 643-649.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.17
-
Alicyclobacillus acidocaldarius

Protein Variants

EC Number Protein Variants Comment Organism
5.4.99.17 D377C/V380E/V381A no detectable cyclization of squalene Alicyclobacillus acidocaldarius
5.4.99.17 E45A reduced enzyme activity Alicyclobacillus acidocaldarius
5.4.99.17 E45D reduced enzyme activity Alicyclobacillus acidocaldarius
5.4.99.17 E45K no enzyme activity Alicyclobacillus acidocaldarius
5.4.99.17 E45Q slightly increased enzyme activity Alicyclobacillus acidocaldarius

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.4.99.17 additional information
-
additional information Km for wild type and mutant enzymes Alicyclobacillus acidocaldarius

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.17 Alicyclobacillus acidocaldarius
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.17 squalene
-
Alicyclobacillus acidocaldarius hop-22(29)-ene
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.4.99.17 additional information
-
wild type and mutant enzymes Alicyclobacillus acidocaldarius