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Information on EC 3.1.7.5 - geranylgeranyl diphosphate diphosphatase
for references in articles please use BRENDA:EC3.1.7.5
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.7 Diphosphoric-monoester hydrolases
3.1.7.5 geranylgeranyl diphosphate diphosphatase
IUBMB Comments
Involved in the biosynthesis of plaunotol. There are two isoenzymes with different ion requirements. Neither require Mg2+ but in addition PII is inhibited by Zn2+, Mn2+ and Co2+. It is not known which isoenzyme is involved in plaunotol biosynthesis.
The expected taxonomic range for this enzyme is: Croton stellatopilosus
showSynonyms
ggpp phosphatase, geranylgeranyl diphosphate phosphatase, prenyl diphosphate phosphatase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
geranylgeranyl diphosphate phosphatase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranylgeranyl diphosphate + H2O = geranylgeraniol + diphosphate
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-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
plaunotol biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphohydrolase
Involved in the biosynthesis of plaunotol. There are two isoenzymes with different ion requirements. Neither require Mg2+ but in addition PII is inhibited by Zn2+, Mn2+ and Co2+. It is not known which isoenzyme is involved in plaunotol biosynthesis.
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CAS REGISTRY NUMBER
COMMENTARY
160995-43-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
farnesyl diphosphate + H2O
farnesol + diphosphate
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Substrates: 11% of the activity with geranylgeranyl diphosphate, isoenzyme PI. 23% of the activity with geranylgeranyl diphosphate, isoenzyme PII
Products: -
Products: -
?
geranyl diphosphate + H2O
geraniol + diphosphate
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Substrates: 7% of the activity with geranylgeranyl diphosphate, isoenzyme PI. 10% of the activity with geranylgeranyl diphosphate, isoenzyme PII
Products: -
Products: -
?
geranylgeranyl phosphate + H2O
geranylgeraniol + phosphate
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Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with isopentenyl diphosphate, isoenzyme PI and PII
Products: -
Products: -
?
geranylgeranyl diphosphate + H2O
geranylgeraniol + diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate + H2O
geranylgeraniol + diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate + H2O
geranylgeraniol + diphosphate
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Substrates: the enzyme is involved in the biosynthesis of plaunotol, a commercial anti-peptic acyclic diterpenoid
Products: -
Products: -
?
geranylgeranyl diphosphate + H2O
geranylgeraniol + diphosphate
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Substrates: formation of geranylgeraniol from geranylgeranyl diphosphate proceeds in the chloroplasts via two successive monodephosphorylation reactions
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
geranylgeranyl diphosphate + H2O
geranylgeraniol + diphosphate
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Substrates: the enzyme is involved in the biosynthesis of plaunotol, a commercial anti-peptic acyclic diterpenoid
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
-
1.0 mM, 18% inhibition of isoenzyme PI, slight activation (1.1fold) of isoenzyme PII
additional information
-
both activities (isoenzyme I and II) are Mg2+-independent
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Co2+
-
1.0 mM, complete inhibition of isoenzyme PII, 21% inhibition of isoenzyme PI
geranylgeranyl diphosphate
-
substrate inhibition above 0.2 mM, isoenzyme PII. Isoenzyme PI shows no substrate inhibition
K+
-
1.0 mM, 18% inhibition of isoenzyme PI, slight activation (1.1fold) of isoenzyme PII
Mn2+
-
1.0 mM, complete inhibition of isoenzyme PII, 4% inhibition of isoenzyme PI
Na+
-
1.0 mM, 23% inhibition of isoenzyme PI, 5% inhibition of isoenzyme PII
Na2MoO4
-
1.0 mM, complete inhibition of isoenzyme PI and isoenzyme PII
Zn2+
-
1.0 mM, complete inhibition of isoenzyme PII, no inhibition of isoenzyme PI
additional information
-
isoenzyme PI shows no substrate inhibition by geranylgeranyl diphosphate, no inhibition by 1.0 mM Zn2+ or K+ and very low inhibition by 1 mM Na+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7.5
5 - 7.5
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pH 5.0: about 65% of maximal activity, pH 7.0: about 60% of maximal activity, isoenzyme II
5 - 7.5
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pH 5.0: about 80% of maximal activity, pH 7.0: about 45% of maximal activity, isoenzyme I
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
deduced amino acid sequence shows 6 hydrophobic transmembrane regions
brenda
Highest Expressing Human Cell Lines
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
232000
-
isoenzyme PI, it is not known which isoenzyme (PI or PII) is involved in plaunotol biosynthesis, gel filtration
30600
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1 * 30600, it is not known which isoenzyme (PI or PII) is involved in plaunotol biosynthesis, isoenzyme PII, SDS-PAGE
34000
-
isoenzyme PII, it is not known which isoenzyme (PI or PII) is involved in plaunotol biosynthesis, gel filtration
58700
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4 * 58700, it is not known which isoenzyme (PI or PII) is involved in plaunotol biosynthesis, isoenzyme PII, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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1 * 30600, it is not known which isoenzyme (PI or PII) is involved in plaunotol biosynthesis, isoenzyme PII, SDS-PAGE
tetramer
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4 * 58700, it is not known which isoenzyme (PI or PII) is involved in plaunotol biosynthesis, isoenzyme PII, SDS-PAGE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of a series of N-terminal deletion mutants based on the locations of the transmembrane regionsand phosphatase motifs. The absence of the first transmembrane region yields a higher expression level than does the full-length cDNA construct, whereas the absence of the first two transmembrane regions prevents expression of the gene construct. The level of activity depends on the length of the expressed protein products. The absence of the first transmembrane region and part of the cytosolic region decreases the phosphatase activity by approximately 40%. The complete absence of both the first transmembrane and cytosolic regions causes a considerable decrease in enzymatic activity
additional information
-
construction of a series of N-terminal deletion mutants based on the locations of the transmembrane regionsand phosphatase motifs. The absence of the first transmembrane region yields a higher expression level than does the full-length cDNA construct, whereas the absence of the first two transmembrane regions prevents expression of the gene construct. The level of activity depends on the length of the expressed protein products. The absence of the first transmembrane region and part of the cytosolic region decreases the phosphatase activity by approximately 40%. The complete absence of both the first transmembrane and cytosolic regions causes a considerable decrease in enzymatic activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nualkaew, N.; De-Eknamkul, W.; Kutchan, T.M.; Zenk, M.H.
Membrane-bound geranylgeranyl diphosphate phosphatases: purification and characterization from Croton stellatopilosus leaves
Phytochemistry
67
1613-1620
2006
Croton stellatopilosus
brenda
Nualkaew, N.; De-Eknamkul, W.; Kutchan, T.; Zenk, M.
Geranylgeraniol formation in Croton stellatopilosus proceeds via successive monodephosphorylations of geranylgeranyl diphosphate
Tetrahedron Lett.
46
8727-8731
2005
Croton stellatopilosus
-
brenda
Nualkaew, N.; Guennewich, N.; Springob, K.; Klamrak, A.; De-Eknamkul, W.; Kutchan, T.M.
Molecular cloning and catalytic activity of a membrane-bound prenyl diphosphate phosphatase from Croton stellatopilosus Ohba
Phytochemistry
91
140-147
2013
Croton stellatopilosus (K4FKJ1), Croton stellatopilosus
brenda
EXTERNAL LINKS (specific for EC-Number 3.1.7.5)
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Release 2023.1 (January 2023)
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