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Literature summary for 4.2.3.19 extracted from

  • Kawaide, H.; Sassa, T.; Kamiya, Y.
    Functional analysis of the two interacting cyclase domains in ent-kaurene synthase from the fungus Phaeosphaeria sp. L487 and a comparison with cyclases from higher plants (2000), J. Biol. Chem., 275, 2276-2280.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
in Escherichia coli as glutathione-S-transferase fusion protein Phaeosphaeria sp.

Protein Variants

Protein Variants Comment Organism
D132A low activity Phaeosphaeria sp.
D320A low activity Phaeosphaeria sp.
D656A no activity Phaeosphaeria sp.
additional information several N- and C-terminal truncated enzymes produced, all found to be inactive Phaeosphaeria sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ent-copalyl diphosphate Phaeosphaeria sp. involved in biosynthesis of gibberellins ent-kaurene + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Phaeosphaeria sp. O13284
-
-
Phaeosphaeria sp. L487 O13284
-
-

Purification (Commentary)

Purification (Comment) Organism
from E. coli Phaeosphaeria sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ent-copalyl diphosphate
-
Phaeosphaeria sp. ent-kaurene + diphosphate
-
?
ent-copalyl diphosphate involved in biosynthesis of gibberellins Phaeosphaeria sp. ent-kaurene + diphosphate
-
?

Synonyms

Synonyms Comment Organism
More part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A) Phaeosphaeria sp.