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Literature summary for 4.2.3.70 extracted from

  • Hartwig, S.; Frister, T.; Alemdar, S.; Li, Z.; Krings, U.; Berger, R.G.; Scheper, T.; Beutel, S.
    Expression, purification and activity assay of a patchoulol synthase cDNA variant fused to thioredoxin in Escherichia coli (2014), Protein Expr. Purif., 97, 61-71.
    View publication on PubMed

Application

Application Comment Organism
synthesis fusion to thioredoxin and careful codon optimization of the eukaryotic sequence improves solubl expression on average by 42% in comparison to an unoptimized, His-tagged construct Pogostemon cablin

Cloned(Commentary)

Cloned (Comment) Organism
expression in Eschrichia coli Pogostemon cablin

Protein Variants

Protein Variants Comment Organism
additional information fusion to thioredoxin and careful codon optimization of the eukaryotic sequence improves solubl expression on average by 42% in comparison to an unoptimized, His-tagged construct Pogostemon cablin

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Pogostemon cablin
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ absolutely required Pogostemon cablin

Organism

Organism UniProt Comment Textmining
Pogostemon cablin Q49SP3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E,6E)-farnesyl diphosphate + H2O
-
Pogostemon cablin patchoulol + diphosphate main product of recombinant enzyme is germacrene A, additional formation of + alpha-bulnesene ?