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Literature summary for 4.2.3.132 extracted from

  • Peters, R.J.; Flory, J.E.; Jetter, R.; Ravn, M.M.; Lee, H.J.; Coates, R.M.; Croteau, R.B.
    Abietadiene synthase from grand fir (Abies grandis): characterization and mechanism of action of the "pseudomature" recombinant enzyme (2000), Biochemistry, 39, 15592-15602.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
truncated abietadiene synthase is expressed in Escherichia coli BL21(DE3) cells Abies grandis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00035
-
(+)-copalyl diphosphate in 50 mM HEPES, pH 7.2, 100 mM KCl, 7.5 mM MgCl2, 0.02 mM MnCl2, at 30°C Abies grandis

Organism

Organism UniProt Comment Textmining
Abies grandis
-
grand fir
-

Purification (Commentary)

Purification (Comment) Organism
type II ceramic hydroxyapatite column chromatography and POROS HQ/M column chromatography Abies grandis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(+)-copalyl diphosphate the enzyme converts geranylgeranyl diphosphate and the intermediate (+)-copalyl diphosphate to a nearly equal mixture of abietadiene (31%), levopimaradiene (34%), and neoabietadiene (28%), as well as to three minor products pimara-8(14),15-diene (3%), palustradiene (2%), and sandaracopimaradiene (2%) Abies grandis ?
-
?

Synonyms

Synonyms Comment Organism
abietadiene synthase cf. EC 4.2.3.18 Abies grandis
NAS
-
Abies grandis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.75
-
(+)-copalyl diphosphate in 50 mM HEPES, pH 7.2, 100 mM KCl, 7.5 mM MgCl2, 0.02 mM MnCl2, at 30°C Abies grandis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2000
-
(+)-copalyl diphosphate in 50 mM HEPES, pH 7.2, 100 mM KCl, 7.5 mM MgCl2, 0.02 mM MnCl2, at 30°C Abies grandis