Any feedback?
No. of entries
Information on EC 2.5.1.93 - 4-hydroxybenzoate geranyltransferase
for references in articles please use BRENDA:EC2.5.1.93
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.5 Transferring alkyl or aryl groups, other than methyl groups
2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
2.5.1.93 4-hydroxybenzoate geranyltransferase
IUBMB Comments
The enzyme is involved in shikonin biosynthesis. It has a strict substrate specificity for geranyl diphosphate and an absolute requirement for Mg2+ .
The enzyme appears in viruses and cellular organisms
- 2.5.1.93
- shikonins
- naphthoquinone
-
lithospermum
- euchroma
- arnebia
- erythrorhizon
-
geranylation
- prenyltransferase
-
hairy
-
royle
- ubiquinone
- boraginaceae
- acetylshikonin
- mevalonate
-
phenylpropanoid
-
flask
- ammonia
-
prenyl
-
contigs
- pyrophosphate
- isobutyrylshikonin
Reaction Schemes
showSynonyms
lepgt1, aepgt6, phb geranyltransferase, p-hydroxybenzoate-m-geranyltransferase, p-hydroxybenzoate:geranyltransferase, aepgt, p-hydroxybenzoate geranyltransferase, diphosphate:4-hydroxybenzoate geranyltransferase, lepgt-1, lepgt, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
geranyl diphosphate:4-hydroxybenzoate 3-geranyltransferase
-
geranyl diphosphate:4-hydroxybenzoate geranyltransferase
-
p-hydroxybenzoate geranyltransferase
PHB geranyltransferase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate + 4-hydroxybenzoate = 3-geranyl-4-hydroxybenzoate + diphosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
shikonin biosynthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
-
Substrates: -
Products: -
Products: -
?
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
Substrates: regulatory enzyme for the biosynthesis of shikonin, a naphthoquinone pigment
Products: -
Products: -
?
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
-
Substrates: regulatory enzyme in the biosynthesis of shikonin
Products: -
Products: -
?
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
Substrates: LePGT1 can utilize only geranyl diphosphate as its prenyl substrate
Products: -
Products: -
?
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
Substrates: the enzyme accepts only geranyl diphosphate and not dimethylallyl diphosphate, farnesyl diphosphate, or geranylgeranyl diphosphate as the substrate
Products: -
Products: -
?
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
Substrates: the enzyme accepts only geranyl-diphosphate and not dimethylallyl diphosphate, farnesyl diphosphate, or geranylgeranyl diphosphate as the substrate
Products: -
Products: -
?
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
-
Substrates: the enzyme is highly specific for geranyl diphosphate and 4-hydroxybenzoate
Products: -
Products: -
?
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
Substrates: LePGT1 reveals high specificity for PHB to give 3-geranyl-4-hydroxybenzoic acid (100%)
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
-
Substrates: -
Products: -
Products: -
?
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
Substrates: regulatory enzyme for the biosynthesis of shikonin, a naphthoquinone pigment
Products: -
Products: -
?
geranyl diphosphate + 4-hydroxybenzoate
3-geranyl-4-hydroxybenzoate + diphosphate
-
Substrates: regulatory enzyme in the biosynthesis of shikonin
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
no activity with Ca2+, Cu2+, and Zn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-chloro-mercuriphenylsulfonic acid
-
0.1 mM, completely inhibits 4HB geranyltransferase activity
iodoacetamide
-
10 mM, completely inhibits 4HB geranyltransferase activity
N-Methylmaleimide
-
10 mM, completely inhibits 4HB geranyltransferase activity
additional information
-
blue light effectively represses the PHB geranyltransferase activity
-
additional information
compounds showing strong competition/inhibition are simple phenols having phenolic OH residues, while carboxylic acid does not seem to influence the enzyme activity. Phenylpropanoid gives no apparent inhibition. No or poor inhibition by benzoate, 2-hydroxybenzoate, 3-hydroxybenzoate, ferulic acid, and 4-coumaric acid
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
0.0184
4-hydroxybenzoate
recombinant enzyme, pH 7.0-7.5, 45°C
0.0022
geranyl diphosphate
pH 7.6, 30°C, mutant enzyme D208E
0.0138
geranyl diphosphate
recombinant enzyme, pH 7.0-7.5, 45°C
0.0365
geranyl diphosphate
pH 7.6, 30°C, mutant enzyme D212E
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0665
recombinant enzyme in crude Sf9 cell extract, pH 7.0-7.5, 45°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2 - 9.3
-
half-maximal activity at pH 6.2 and at pH 9.3, Tris-HCl buffer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the mRNA of the LePGT-1 gene is undetectable in aerial plant tissues, and is exclusively detected in root tissues, similar to shikonin accumulation
brenda
the mRNA of the LePGT-2 gene is undetectable in aerial plant tissues, and is exclusively detected in root tissues, similar to shikonin accumulation
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the phylogenetic tree shows that 4-hydroxybenzoate geranyltransferase (PGT) and 4-hydroxybenzoate polyprenyltransferase (PPT) belong to two different clades
metabolism
physiological function
additional information
LePGT1 is a model membrane-bound aromatic substrate prenyltransferase
metabolism
-
the enzyme catalyzes a key step in the geranyl diphosphate pathway for shikonins biosynthesis, and its couples the mevalonate and the diphosphate pathways, overview
metabolism
the reaction catalyzed by lePGT-1 plays as a competing pathway on two substrates of the Q8 synthesis pathway, namely at IPP and 4-hydroxybenzoate
metabolism
-
the enzyme plays an important role in the biosynthesis pathways of shikonin derivatives
physiological function
-
regulatory enzyme in the biosynthesis of shikonin
physiological function
the enzyme is involved in the biosynthesis of a red naphthoquinone pigment, shikonin
physiological function
the enzyme is part of a metabolic strategy to further controll the respiratory levels in CoQ8 biosynthesis-deficient Escherichia coli strains, this metabolic strategy can lead to fine-tuning of aerobic lactate accumulation. The lactate and acetate concentrations increase with increasing enzyme levels, as does the cell density, while glucose concentration decreases, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PGT1_LITER
307
6
34319
Swiss-Prot
other Location (Reliability: 3)
PGT2_LITER
306
6
34222
Swiss-Prot
other Location (Reliability: 3)
A0A2P6QDR0_ROSCH
76
1
8451
TrEMBL
other Location (Reliability: 4)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the enzyme contains contains multiple transmembrane alpha-helices
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D212A
D87A
additional information
D212A
site-directed mutagenesis, the mutant shows almost no expression of the recombinant protein
D87A
site-directed mutagenesis, the mutant can be be successfully expressed, but is catalytically inactive
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
additional information
the substitution of aspartate with alanine, especially D87 and D212, causes a dramatic decrease in enzyme activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
storage at pH 5 or pH 7 results in a loss of activity between 20% and 30% in 8 days
706366
6
-
at pH 6, the enzyme can be stored in the presence of 1.5 mM digitonin, 10% glycerol and 2 mM DTT at 4°C for two weeks with minimal loss of activity
706366
7
-
storage at pH 5 or pH 7 results in a loss of activity between 20% and 30% in 8 days
706366
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 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.
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Of various detergents examined, digitonin is the most suitable for the solubilization of the enzyme
-
recombinant C-terminally His-tagged LePGT1 41.3fold from Spodoptera frugiperda Sf9 cells by improved detergent solubilization with 6 mM sodium deoxycholate, and nickel affinity chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
expression in Saccharomyces cerevisiae WAT11U strain and in a high yield monoterpene strain (HMT1). AePGT6 shows higher geranyltransferase activity in yeas than AePGT4 and AePGT
functional expression of LePGTs in a yeast COQ2 disruptant
recombinant expression in Escherichia coli coenzyme Q8 biosynthesis-deficient strains, HW108 and HW109, which contain mutations in ubiE and ubiG, respectively. Gene lePGT-1 gene is amplified and cloned into the expression vector, pBAD33, to form pBlePGT, the fine-tuning of the expression of lePGT-1 in the ubiquinone-deficient strains, HW108 and HW109, to control the electron transfer chain is investigated by adding different concentrations of the inducer arabinose at 0-20 mM under fully aerobic conditions
recombinant expression of C-terminally His-tagged LePGT1 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection method
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gaisser, S.; Heide, L.
Inhibition and regulation of shikonin biosynthesis in suspension cultures of Lithospermum
Phytochemistry
41
1065-1072
1996
Lithospermum erythrorhizon
-
brenda
Ohara, K.; Muroya, A.; Fukushima, N.; Yazaki, K.
Functional characterization of LePGT1, a membrane-bound prenyltransferase involved in the geranylation of p-hydroxybenzoic acid
Biochem. J.
421
231-241
2009
Lithospermum erythrorhizon (Q8W405)
brenda
Yazaki, K.; Kunihisa, M.; Fujisaki, T.; Sato, F.
Geranyl diphosphate:4-hydroxybenzoate geranyltransferase from Lithospermum erythrorhizon. Cloning and characterization of a ket enzyme in shikonin biosynthesis
J. Biol. Chem.
277
6240-6246
2001
Lithospermum erythrorhizon (Q8W404), Lithospermum erythrorhizon (Q8W405), Lithospermum erythrorhizon
brenda
Yamaga, Y.; Nakanishi, K.; Fukui, H.; Tabata, M.
Intracellular localization of p-hydroxybenzoate geranyltransferase, a key enzyme involved in shikonin biosynthesis
Phytochemistry
32
633-636
1993
Lithospermum erythrorhizon
-
brenda
Mhlenweg, A.; Melzer, M.; Li, S.M.; Heide, L.
4-Hydroxybenzoate 3-geranyltransferase from Lithospermum erythrorhizon: purification of a plant membrane-bound prenyltransferase
Planta
205
407-413
1998
Lithospermum erythrorhizon
brenda
Singh, R.S.; Gara, R.K.; Bhardwaj, P.K.; Kaachra, A.; Malik, S.; Kumar, R.; Sharma, M.; Ahuja, P.S.; Kumar, S.
Expression of 3-hydroxy-3-methylglutaryl-CoA reductase, p-hydroxybenzoate-m-geranyltransferase and genes of phenylpropanoid pathway exhibits positive correlation with shikonins content in arnebia [Arnebia euchroma (Royle) Johnston]
BMC Mol. Biol.
11
88
2010
Arnebia euchroma
brenda
Wu, H.; Bennett, G.N.; San, K.Y.
Metabolic control of respiratory levels in coenzyme Q biosynthesis-deficient Escherichia coli strains leading to fine-tune aerobic lactate fermentation
Biotechnol. Bioeng.
112
1720-1726
2015
Lithospermum erythrorhizon (Q8W405), Lithospermum erythrorhizon
brenda
Ohara, K.; Mito, K.; Yazaki, K.
Homogeneous purification and characterization of LePGT1 - a membrane-bound aromatic substrate prenyltransferase involved in secondary metabolism of Lithospermum erythrorhizon
FEBS J.
280
2572-2580
2013
Lithospermum erythrorhizon (Q8W405)
-
brenda
Wang, S.; Wang, R.; Liu, T.; Zhan, Z.; Kang, L.; Wang, Y.; Lv, C.; Werck-Reichhart, D.; Guo, L.; Huang, L.
Production of 3-geranyl-4-hydroxybenzoate acid in yeast, an important intermediate of shikonin biosynthesis pathway
FEMS Yeast Res.
17
fox065
2017
Arnebia euchroma (A0A168S819), Arnebia euchroma (A0A168S850), Arnebia euchroma (Q0QFI7), Arnebia euchroma
brenda
Liu, T.; Lv, C.; Wang, S.; Yang, W.; Guo, L.
Transcriptome-based gene mining and bioinformatics analysis of p-hydroxybenzoate geranyltransferase genes in Arnebia euchroma
Zhongguo Zhong Yao Za Zhi
41
1422-1429
2016
Arnebia euchroma
brenda
EXTERNAL LINKS (specific for EC-Number 2.5.1.93)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
