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Literature summary for 1.14.14.174 extracted from

  • Yamamoto. H.; Inoue, K.; Li, S.M.; Heide, L.
    Geranylhydroquinone 3"-hydroxylase, a cytochrome P-450 monooxygenase from Lithospermum erythrorhizon cell suspension cultures (2000), Planta, 210, 312-317.
    View publication on PubMed
Search for more literature for 1.14.14.174

Activating Compound

Activating Compound Comment Organism Structure
cytochrome P-450 involved in activity Lithospermum erythrorhizon

General Stability

General Stability Organism
addition of glycerol (20%, v/v) to the microsomal fraction before freezing results in the loss of 80% of the activity Lithospermum erythrorhizon
stable against freezing Lithospermum erythrorhizon

Inhibitors

Inhibitors Comment Organism Structure
Ancymidol 1 mM, 38% inhibition Lithospermum erythrorhizon
CO inhibitory effect of CO is reversed by illumination Lithospermum erythrorhizon
cytochrome c 0.01 mM, 96% inhibition Lithospermum erythrorhizon
ketoconazole 1 mM, 62% inhibition Lithospermum erythrorhizon
Metyrapone 1 mM, 14% inhibition Lithospermum erythrorhizon

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0015
-
 geranylhydroquinone pH 7.4, 30°C, microsomal fraction Lithospermum erythrorhizon

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Lithospermum erythrorhizon
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
geranylhydroquinone + [reduced NADPH-hemoprotein reductase] + O2 Lithospermum erythrorhizon likely to be involved in shikonin and dihydroechinofuran biosynthesis 3''-hydroxygeranylhydroquinone + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Lithospermum erythrorhizon
-
 Sieb. et Zucc.
-

Source Tissue

Source Tissue Comment Organism Textmining
cell suspension culture
-
 Lithospermum erythrorhizon
-

Storage Stability

Storage Stability Organism
-70°C, 1 month, microsomal protein retains 82% of the original activity Lithospermum erythrorhizon

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
geranylhydroquinone + [reduced NADPH-hemoprotein reductase] + O2 likely to be involved in shikonin and dihydroechinofuran biosynthesis Lithospermum erythrorhizon 3''-hydroxygeranylhydroquinone + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
geranylhydroquinone + [reduced NADPH-hemoprotein reductase] + O2 hydroxylation takes place specifically at position 3'', i.e. at the methyl group involved in the cyclization reaction. The reaction velocity obtained with 3-geranyl-4-hydroxybenzoic acid is more than 100 times lower than that obtained with geranylhydro-quinone Lithospermum erythrorhizon 3''-hydroxygeranylhydroquinone + [oxidized NADPH-hemoprotein reductase] + H2O proton/proton correlation spectroscopic and proton/proton long-range correlation spectroscopic studies confirm that hydroxylation takes place specifically at position 3'' ?

Synonyms

Synonyms Comment Organism
GHQ 3''-hydroxylase
-
 Lithospermum erythrorhizon

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
 Lithospermum erythrorhizon

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 activity in K-phosphate buffer at pH 7.4 is only 40% of that observed in Tris-HCl buffer Lithospermum erythrorhizon

pH Range

pH Minimum pH Maximum Comment Organism
6.7 8.3 50% of maximal activiyt at pH 6.7 and pH 8.3. Tris-Cl buffer Lithospermum erythrorhizon

Cofactor

Cofactor Comment Organism Structure
NADPH required, could not be replaced by NADH, FAD or FMN. The optimal concentration of NADPH for this reaction is between 1 and 5 mM Lithospermum erythrorhizon