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Literature summary 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)

EC Number Cloned (Comment) Organism
4.2.3.19 in Escherichia coli as glutathione-S-transferase fusion protein Phaeosphaeria sp.
5.5.1.13 expression in Escherichia coli of a recombinant GST fused enzyme Cucurbita maxima
5.5.1.13 expression in Escherichia coli of a recombinant GST fused enzyme Phaeosphaeria sp.

Protein Variants

EC Number Protein Variants Comment Organism
4.2.3.19 D132A low activity Phaeosphaeria sp.
4.2.3.19 D320A low activity Phaeosphaeria sp.
4.2.3.19 D656A no activity Phaeosphaeria sp.
4.2.3.19 additional information several N- and C-terminal truncated enzymes produced, all found to be inactive Phaeosphaeria sp.
5.5.1.13 D320A the mutation leads to complete enzyme activity Phaeosphaeria sp.
5.5.1.13 D656A the mutation causes a small reduction in activity Phaeosphaeria sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.5.1.13 EDTA inhibits activity in cell free extract containing the enzyme Phaeosphaeria sp.
5.5.1.13 additional information substrate inhibition Cucurbita maxima

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.5.1.13 0.00023
-
 copalyl diphosphate at pH 8 Phaeosphaeria sp.
5.5.1.13 0.00873
-
 geranylgeranyl diphosphate at pH 8 Phaeosphaeria sp.
5.5.1.13 0.0169
-
 geranylgeranyl diphosphate at pH 8 Cucurbita maxima

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.5.1.13 106000
-
 calculated from amino acid sequence Phaeosphaeria sp.

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.19 Phaeosphaeria sp. O13284
-
-
4.2.3.19 Phaeosphaeria sp. L487 O13284
-
-
5.5.1.13 Cucurbita maxima
-
 pumpkin
-
5.5.1.13 Phaeosphaeria sp. O13284 from mycelia
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.3.19 from E. coli Phaeosphaeria sp.
5.5.1.13 cell free extract Phaeosphaeria sp.
5.5.1.13 recombinant enzyme, using Sepharose 4B glutathione affinity resin and SDS PAGE electrophoresis Phaeosphaeria sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.5.1.13 0.00075
-
 at pH 8 Phaeosphaeria sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.19 ent-copalyl diphosphate
-
 Phaeosphaeria sp. ent-kaurene + diphosphate
-
 ?
4.2.3.19 ent-copalyl diphosphate involved in biosynthesis of gibberellins Phaeosphaeria sp. ent-kaurene + diphosphate
-
 ?
5.5.1.13 copalyl diphosphate bifunctional enzyme Phaeosphaeria sp. ent-kaurene + diphosphate
-
 ?
5.5.1.13 geranylgeranyl diphosphate
-
 Cucurbita maxima copalyl diphosphate
-
 ?
5.5.1.13 geranylgeranyl diphosphate
-
 Phaeosphaeria sp. copalyl diphosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.3.19 additional information 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.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.5.1.13 0.00117
-
 copalyl diphosphate at pH 8 Phaeosphaeria sp.
5.5.1.13 0.0308
-
 geranylgeranyl diphosphate at pH 8 Phaeosphaeria sp.
5.5.1.13 0.035
-
 geranylgeranyl diphosphate at pH 8 Cucurbita maxima