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Literature summary extracted from

  • Eslami, H.; Mohtashami, S.K.; Basmanj, M.T.; Rahati, M.; Rahimi, H.
    An in-silico insight into the substrate binding characteristics of the active site of amorpha-4,11-diene synthase, a key enzyme in artemisinin biosynthesis (2017), J. Mol. Model., 23, 202 .
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.3.24 Mg2+ contains three Mg2+ ions Artemisia annua

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.3.24 (2E,6E)-farnesyl diphosphate Artemisia annua
-
amorpha-4,11-diene + diphosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.24 Artemisia annua A2TEY7
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.24 (2E,6E)-farnesyl diphosphate
-
Artemisia annua amorpha-4,11-diene + diphosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
4.2.3.24 ADS
-
Artemisia annua
4.2.3.24 amorphadiene synthase
-
Artemisia annua