Information on EC 2.5.1.93 - 4-hydroxybenzoate geranyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.5.1.93
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RECOMMENDED NAME
GeneOntology No.
4-hydroxybenzoate geranyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate + 4-hydroxybenzoate = 3-geranyl-4-hydroxybenzoate + diphosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
shikonin biosynthesis
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Ubiquinone and other terpenoid-quinone biosynthesis
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate:4-hydroxybenzoate 3-geranyltransferase
The enzyme is involved in shikonin biosynthesis. It has a strict substrate specificity for geranyl diphosphate and an absolute requirement for Mg2+ [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the enzyme catalyzes a key step in the geranyl diphosphate pathway for shikonins biosynthesis, and its couples the mevalonate and the diphosphate pathways, overview
physiological function
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regulatory enzyme in the biosynthesis of shikonin
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required, optimal concentration: 20-50 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloro-mercuriphenylsulfonic acid
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0.1 mM, completely inhibits 4HB geranyltransferase activity
iodoacetamide
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10 mM, completely inhibits 4HB geranyltransferase activity
N-Methylmaleimide
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10 mM, completely inhibits 4HB geranyltransferase activity
additional information
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blue light effectively represses the PHB geranyltransferase activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0103 - 0.0664
4-hydroxybenzoate
0.0022 - 0.0459
geranyl diphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
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in Bis-Tris-HCl buffer
8.5
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in Tris-HCl buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 9.3
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half-maximal activity at pH 6.2 and at pH 9.3, Tris-HCl buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 63
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half-maximal activity at 35C and at 63C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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derived from germinating seeds
Manually annotated by BRENDA team
the mRNA of the LePGT-1 gene is undetectable in aerial plant tissues, and is exclusively detected in root tissues, similar to shikonin accumulation; the mRNA of the LePGT-2 gene is undetectable in aerial plant tissues, and is exclusively detected in root tissues, similar to shikonin accumulation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
341000
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gel filtration
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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at pH 4 or 8, all activtiy is lost quickly
706366
5
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storage at pH 5 or pH 7 results in a loss of activity between 20% and 30% in 8 days
706366
6
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at pH 6, the enzyme can be stored in the presence of 1.5 mM digitonin, 10% glycerol and 2 mM DTT at 4C for two weeks with minimal loss of activity
706366
7
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storage at pH 5 or pH 7 results in a loss of activity between 20% and 30% in 8 days
706366
8
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at pH 4 or 8, all activtiy is lost quickly
706366
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, in the presence of 10% glycerol, frozen enzyme preparations are stable upon storage for at least two months. Protease inhibitors directed against serin-, carboxyl-, and metalloproteases such as PMSF, 1,2-epoxy-3-(4-nitrophenoxy)-propane or EGTA do not increase the stability of the enzyme solution.
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Of various detergents examined, digitonin is the most suitable for the solubilization of the enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
all point mutants and chimeric enzymes are constitutively expressed in Saccharomyces cerevisiae containing a disrupted copy of the COQ2 gene
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functional expression of LePGTs in a yeast COQ2 disruptant; functional expression of LePGTs in a yeast COQ2 disruptant
PGT expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
blue light represses activity
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mevinolin downregulates PGT in vivo
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white light induces activity
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D208A
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no activity
D211A
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enzyme activity is 1.12% of wild-type activity
D212A
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enzyme activity is 0.11% of wild-type activity
D84A
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enzyme activity is 1.28% of wild-type activity
D87A
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no activity
D91A
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no activity
K152A
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enzyme activity is 0.15% of wild-type activity
K229A
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enzyme activity is 12.9% of wild-type activity
N83A
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enzyme activity is 0.82% of wild-type activity
Q207A
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enzyme activity is 2.31% of wild-type activity
R153A
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enzyme activity is 81.6% of wild-type activity
R76A
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enzyme activity is 0.26% of wild-type activity
R96A
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enzyme activity is 0.22% of wild-type activity
S219A
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enzyme activity is 14.7% of wild-type activity
additional information
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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