Information on EC 4.1.1.98 - 4-hydroxy-3-polyprenylbenzoate decarboxylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.1.1.98
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RECOMMENDED NAME
GeneOntology No.
4-hydroxy-3-polyprenylbenzoate decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 4-hydroxy-3-polyprenylbenzoate = a 2-polyprenylphenol + CO2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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plastoquinol-9 biosynthesis II
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ubiquinol-10 biosynthesis (prokaryotic)
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ubiquinol-7 biosynthesis (prokaryotic)
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ubiquinol-8 biosynthesis (prokaryotic)
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ubiquinol-9 biosynthesis (prokaryotic)
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Ubiquinone and other terpenoid-quinone biosynthesis
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ubiquinone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxy-3-polyprenylbenzoate carboxy-lyase
The enzyme catalyses a step in prokaryotic ubiquinone biosynthesis, as well as in plastoquinone biosynthesis in cyanobacteria. The enzyme can accept substrates with different polyprenyl tail lengths in vitro, but uses a specific length in vivo, which is determined by the polyprenyl diphosphate synthase that exists in the specific organism. It requires a prenylated flavin cofactor that is produced by EC 2.5.1.129, flavin prenyltransferase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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the enzyme is involved in the decarboxylation step in coenzyme Q biosynthesis
physiological function
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the enzyme is required for production of coenzyme Q8 and growth on succinate media
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-octaprenyl-4-hydroxybenzoate
2-octaprenylphenol + CO2
show the reaction diagram
4-hydroxy-3-farnesylbenzoate
? + CO2
show the reaction diagram
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highest activity with 4-hydroxy-3-farnesylbenzoate
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?
4-hydroxy-3-geranylgeranylbenzoate
? + CO2
show the reaction diagram
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?
a 4-hydroxy-3-polyprenylbenzoate
a 2-polyprenylphenol + CO2
show the reaction diagram
additional information
?
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very low specific activity with 4-hydroxy-3-octaprenylbenzoate
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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
a 4-hydroxy-3-polyprenylbenzoate
a 2-polyprenylphenol + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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the enzyme does not bind FMN
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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contains a Mg2+ binding site
Mn2+
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for optimal activity the enzyme requires Mn2+
additional information
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the addition of divalent cations does not stimulate the enzyme activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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complete inhibition at 1 mM
Protamine sulfate
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treatment of cell extract with 90% of the volume of protamine sulfate solution needed to completely precipitate nucleic acids results in a loss of more than 95% of the total enzyme activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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slight stimulation of activity at 10 mM
dithiothreitol
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maximal stimulation of activity at about 10 mM
glutathione
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slight stimulation of activity at 10 mM
lipoate
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slight (20%) stimulation of activity at 10 mM
methanol
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strong stimulation
Phospholipid
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additional information
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not activated by thiamine diphosphate, coenzyme A, pyridoxamine phosphate, pyridoxall 5'-phosphate, biotin, ascorbic acid, NADH, NADPH, folic acid, FAD, FMN, or glutamate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
calculated from amino acid sequence
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22552
12 * 22552, calculated from amino acid sequence
23175
12 * 23175, electron spray ionization mass spectrometry
23183
12 * 23183, calculated from amino acid sequence
57614
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2 * 57614, SeMet-substituted protein, calculated from amino acid sequence
256300
gel filtration
295000
gel filtration
340000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
12 * 22552, calculated from amino acid sequence
homodimer
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2 * 57614, SeMet-substituted protein, calculated from amino acid sequence
homododecamer
12 * 23175, electron spray ionization mass spectrometry; 12 * 23183, calculated from amino acid sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M trisodium citrate pH 5.4, 0.5 M ammonium sulfate, 1.2 M lithium sulfate
hanging drop vapor diffusion method, using 15% (w/v) PEG 4000, 0.2 M LiSO4, and 0.1 M Hepes buffer (pH 7.0)
sitting drop vapor diffusion method, using 1 M (NH4)2SO4, 0.1 M Bis-Tris, pH 5.5, 1% (w/v) PEG 3350 or 0.1 M HEPES, pH 7.5, 0.2 M MgCl2, 10% (w/v) PEG 400
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose bead chromatography and Sephacryl S200 gel filtration
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Ni-NTA resin column chromatography and Superdex 200 gel filtration
Ni-NTA resin column chromatography and Superose 12 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli ubiX and ubiD deletion mutant
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
V47S
a FMN-free mutant
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