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Literature summary for 2.5.1.67 extracted from

  • Christianson, D.W.
    Roots of biosynthetic diversity (2007), Science, 316, 60-61.
    View publication on PubMed
Search for more literature for 2.5.1.67

Cloned(Commentary)

Cloned (Comment) Organism
expression of mutant chimeric CPPase-FPPase enzyme in Escherichia coli Artemisia spiciformis

Protein Variants

Protein Variants Comment Organism
additional information construction of mutant enzymes as CPPase-FPPase chimeras with the larger domains of CPPase substituted for FPPase in the Artemisia tridentata enzyme, the CPPase-FPPase chimeras are biosynthetically more promiscuous than either native CPPase or FPPase as a result of a reshaped template for substrate binding, which permits alternative trajectories for intermolecular carbon-carbon bond formation, overview Artemisia spiciformis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 dimethylallyl diphosphate Artemisia spiciformis multistep cyclization cascade, biosynthesic pathway, and family tree of terpenomic diversity, overview diphosphate + chrysanthemyl diphosphate
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 ?

Organism

Organism UniProt Comment Textmining
Artemisia spiciformis
-
 big sagebrush
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 dimethylallyl diphosphate
-
 Artemisia spiciformis diphosphate + chrysanthemyl diphosphate
-
 ?
2 dimethylallyl diphosphate multistep cyclization cascade, biosynthesic pathway, and family tree of terpenomic diversity, overview Artemisia spiciformis diphosphate + chrysanthemyl diphosphate
-
 ?

Subunits

Subunits Comment Organism
More CPPase larger domain structure, modeling, overview Artemisia spiciformis

Synonyms

Synonyms Comment Organism
CPPase
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 Artemisia spiciformis