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Literature summary extracted from

  • Fischereder, E.; Pressnitz, D.; Kroutil, W.; Lutz, S.
    Engineering strictosidine synthase: rational design of a small, focused circular permutation library of the beta-propeller fold enzyme (2014), Bioorg. Med. Chem., 22, 5633-5637.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.3.2 STR gene, expresssion of wild-type enzyme and mutant constructs in Escherichia coli strain BL21(DE3)pLysS Rauvolfia serpentina

Protein Variants

EC Number Protein Variants Comment Organism
4.3.3.2 additional information construction of a STR tandem gene sequence, that serves as template for the preparation of circular permutated STR variants is assembled in pET17b using a truncated version of the STR gene, the N-terminal 28 amino acid residues in STR which constitutes the native signal sequence, as well as the unstructured 11 amino acids at the C-terminus are deleted, leaving a 915-nucleotide truncated version of STR, several truncated variants all show reduced activity compared to the wild-type enzyme, overview Rauvolfia serpentina

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.3.2 tryptamine + secologanin Rauvolfia serpentina the enzyme is as amine lyases and catalyzes a Pictet–Spengler-type condensation between tryptamine and the aldehyde secologanin which leads to the formation of (S)-strictosidine 3-alpha(S)-strictosidine + H2O
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Organism

EC Number Organism UniProt Comment Textmining
4.3.3.2 Rauvolfia serpentina
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.3.2 tryptamine + secologanin
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 Rauvolfia serpentina 3-alpha(S)-strictosidine + H2O
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4.3.3.2 tryptamine + secologanin the enzyme is as amine lyases and catalyzes a Pictet–Spengler-type condensation between tryptamine and the aldehyde secologanin which leads to the formation of (S)-strictosidine Rauvolfia serpentina 3-alpha(S)-strictosidine + H2O
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 ?

Subunits

EC Number Subunits Comment Organism
4.3.3.2 More the enzyme is a six bladed beta-propeller protein Rauvolfia serpentina

Synonyms

EC Number Synonyms Comment Organism
4.3.3.2 str
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 Rauvolfia serpentina

General Information

EC Number General Information Comment Organism
4.3.3.2 evolution strictosidine synthases belong to the beta-propeller fold family characterized by an all-beta architecture with four to eight blades, each consisting of four antiparallel beta-sheets, arranged around a pseudo symmetry axis Rauvolfia serpentina
4.3.3.2 additional information the six bladed beta-propeller protein has two regions which cover the enzyme active site. The observed activity changes suggest important roles of both regions in protein folding, stability and catalysis Rauvolfia serpentina
4.3.3.2 physiological function strictosidine synthases catalyze the formation of strictosidine, a key intermediate in the biosynthesis of a large variety of monoterpenoid indole alkaloids Rauvolfia serpentina