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Literature summary for 5.4.99.17 extracted from

  • Sato, T.; Hoshino, T.
    Functional analysis of the DXDDTA motif in squalene-hopene cyclase by site-directed mutagenesis experiments: initiation site of the polycyclization reaction and stabilization site of the carbocation intermediate of the initially cyclized A-ring (1999), Biosci. Biotechnol. Biochem., 63, 2189-2198.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
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 Alicyclobacillus acidocaldarius

Protein Variants

Protein Variants Comment Organism
additional information various mutations of conserved amino acid residues Alicyclobacillus acidocaldarius

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Alicyclobacillus acidocaldarius
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-
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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 specific activities for wild type and mutant enzymes Alicyclobacillus acidocaldarius

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information overview of cyclization products of wild type and mutant enzymes Alicyclobacillus acidocaldarius ?
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 ?
squalene
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 Alicyclobacillus acidocaldarius hop-22(29)-ene
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 ?

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information wild type and mutant enzymes Alicyclobacillus acidocaldarius