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Literature summary for 2.3.1.160 extracted from

  • Stoeckigt, J.; Panjikar, S.; Ruppert, M.; Barleben, L.; Ma, X.; Loris, E.; Hill, M.
    The molecular architecture of major enzymes from ajmaline biosynthetic pathway (2007), Phytochem. Rev., 6, 15-34.
No PubMed abstract available
Search for more literature for 2.3.1.160

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Rauvolfia serpentina

Crystallization (Commentary)

Crystallization (Comment) Organism
using the hanging-drop vapour-diffusion method Rauvolfia serpentina

Protein Variants

Protein Variants Comment Organism
D164A reduction in enzyme activity Rauvolfia serpentina
D32A reduction in enzyme activity Rauvolfia serpentina
D362A reduction in enzyme activity Rauvolfia serpentina
H160A reduction in enzyme activity Rauvolfia serpentina
S29A reduction in enzyme activity Rauvolfia serpentina

Organism

Organism UniProt Comment Textmining
Rauvolfia serpentina
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-
-

Purification (Commentary)

Purification (Comment) Organism
of the recombinant protein by his-tag affinity column chromatography Rauvolfia serpentina

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
16-epi-vellosimine + acetyl-CoA VS responsible for generation of the basic carbon skeleton of the target compound ajmaline, His160 and Asp164 are the most important amino acids for the catalytic process, His-X-X-X-Asp sequence together with Asp-Phe-Gly-Trp-Gly are highly conserved motifs in acyltransferases Rauvolfia serpentina vinorine + CoA
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 ?

Synonyms

Synonyms Comment Organism
vinorine synthase a member of the BAHD enzyme super-family, benzylalcohol acetyl-, anthocyanin-O-hydroxy-cinnamoyl-, anthranilate-N-hydroxy-cinnamoyl-benzoyl- and deacetylvindoline acetyl transferase, involved in synthesis of ajmaline Rauvolfia serpentina
VS
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 Rauvolfia serpentina