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Literature summary for 2.5.1.93 extracted from

  • Ohara, K.; Muroya, A.; Fukushima, N.; Yazaki, K.
    Functional characterization of LePGT1, a membrane-bound prenyltransferase involved in the geranylation of p-hydroxybenzoic acid (2009), Biochem. J., 421, 231-241.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
all point mutants and chimeric enzymes are constitutively expressed in Saccharomyces cerevisiae containing a disrupted copy of the COQ2 gene Lithospermum erythrorhizon

Protein Variants

Protein Variants Comment Organism
D208A no activity Lithospermum erythrorhizon
D211A enzyme activity is 1.12% of wild-type activity Lithospermum erythrorhizon
D212A enzyme activity is 0.11% of wild-type activity Lithospermum erythrorhizon
D84A enzyme activity is 1.28% of wild-type activity Lithospermum erythrorhizon
D87A no activity Lithospermum erythrorhizon
D91A no activity Lithospermum erythrorhizon
K152A enzyme activity is 0.15% of wild-type activity Lithospermum erythrorhizon
K229A enzyme activity is 12.9% of wild-type activity Lithospermum erythrorhizon
additional information the amino acid residues of LePGT1 critical for the enzymatic activity and the region responsible for the binding of the substrates are elucidated by mutational analysis. Substrate specificity is analysed using chimeric enzymes derived from LePGT1 and UbiA (EC 2.5.1.39). In vitro and in vivo analysis of the chimeras suggests that the determinant region for this specificity is within 130 amino acids of the N-terminal Lithospermum erythrorhizon
N83A enzyme activity is 0.82% of wild-type activity Lithospermum erythrorhizon
Q207A enzyme activity is 2.31% of wild-type activity Lithospermum erythrorhizon
R153A enzyme activity is 81.6% of wild-type activity Lithospermum erythrorhizon
R76A enzyme activity is 0.26% of wild-type activity Lithospermum erythrorhizon
R96A enzyme activity is 0.22% of wild-type activity Lithospermum erythrorhizon
S219A enzyme activity is 14.7% of wild-type activity Lithospermum erythrorhizon

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0022
-
geranyl diphosphate pH 7.6, 30°C, mutant enzyme D208E Lithospermum erythrorhizon
0.0213
-
4-hydroxybenzoate pH 7.6, 30°C, mutant enzyme D212E Lithospermum erythrorhizon
0.0295
-
geranyl diphosphate pH 7.6, 30°C, wild-type enzyme Lithospermum erythrorhizon
0.0305
-
4-hydroxybenzoate pH 7.6, 30°C, mutant enzyme D208E Lithospermum erythrorhizon
0.0365
-
geranyl diphosphate pH 7.6, 30°C, mutant enzyme D212E Lithospermum erythrorhizon
0.0664
-
4-hydroxybenzoate pH 7.6, 30°C, wild-type enzyme Lithospermum erythrorhizon

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Lithospermum erythrorhizon 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
geranyl diphosphate + 4-hydroxybenzoate Lithospermum erythrorhizon regulatory enzyme for the biosynthesis of shikonin, a naphthoquinone pigment 3-geranyl-4-hydroxybenzoate + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Lithospermum erythrorhizon Q8W405
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
geranyl diphosphate + 4-hydroxybenzoate regulatory enzyme for the biosynthesis of shikonin, a naphthoquinone pigment Lithospermum erythrorhizon 3-geranyl-4-hydroxybenzoate + diphosphate
-
?
geranyl diphosphate + 4-hydroxybenzoate LePGT1 can utilize only geranyl diphosphate as its prenyl substrate Lithospermum erythrorhizon 3-geranyl-4-hydroxybenzoate + diphosphate
-
?

Synonyms

Synonyms Comment Organism
LePGT1
-
Lithospermum erythrorhizon

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
assay at Lithospermum erythrorhizon