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EC Tree
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
Synonyms
ggpp phosphatase, geranylgeranyl diphosphate phosphatase, prenyl diphosphate phosphatase,
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geranylgeranyl diphosphate phosphatase
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prenyl diphosphate phosphatase
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geranylgeranyl diphosphate + H2O = geranylgeraniol + diphosphate
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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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farnesyl diphosphate + H2O
farnesol + diphosphate
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11% of the activity with geranylgeranyl diphosphate, isoenzyme PI. 23% of the activity with geranylgeranyl diphosphate, isoenzyme PII
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geranyl diphosphate + H2O
geraniol + diphosphate
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7% of the activity with geranylgeranyl diphosphate, isoenzyme PI. 10% of the activity with geranylgeranyl diphosphate, isoenzyme PII
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geranylgeranyl diphosphate + H2O
geranylgeraniol + diphosphate
geranylgeranyl phosphate + H2O
geranylgeraniol + phosphate
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additional information
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no activity with isopentenyl diphosphate, isoenzyme PI and PII
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geranylgeranyl diphosphate + H2O
geranylgeraniol + diphosphate
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geranylgeranyl diphosphate + H2O
geranylgeraniol + diphosphate
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geranylgeranyl diphosphate + H2O
geranylgeraniol + diphosphate
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the enzyme is involved in the biosynthesis of plaunotol, a commercial anti-peptic acyclic diterpenoid
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geranylgeranyl diphosphate + H2O
geranylgeraniol + diphosphate
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formation of geranylgeraniol from geranylgeranyl diphosphate proceeds in the chloroplasts via two successive monodephosphorylation reactions
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geranylgeranyl diphosphate + H2O
geranylgeraniol + diphosphate
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the enzyme is involved in the biosynthesis of plaunotol, a commercial anti-peptic acyclic diterpenoid
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K+
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1.0 mM, 18% inhibition of isoenzyme PI, slight activation (1.1fold) of isoenzyme PII
additional information
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both activities (isoenzyme I and II) are Mg2+-independent
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Co2+
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1.0 mM, complete inhibition of isoenzyme PII, 21% inhibition of isoenzyme PI
geranylgeranyl diphosphate
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substrate inhibition above 0.2 mM, isoenzyme PII. Isoenzyme PI shows no substrate inhibition
K+
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1.0 mM, 18% inhibition of isoenzyme PI, slight activation (1.1fold) of isoenzyme PII
Mn2+
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1.0 mM, complete inhibition of isoenzyme PII, 4% inhibition of isoenzyme PI
Na+
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1.0 mM, 23% inhibition of isoenzyme PI, 5% inhibition of isoenzyme PII
Na2MoO4
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1.0 mM, complete inhibition of isoenzyme PI and isoenzyme PII
Zn2+
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1.0 mM, complete inhibition of isoenzyme PII, no inhibition of isoenzyme PI
additional information
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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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0.1 - 0.2
geranylgeranyl diphosphate
0.1
geranylgeranyl diphosphate
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pH 7.0, 30°C, isoenzyme II
0.2
geranylgeranyl diphosphate
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pH 7.0, 30°C, isoenzyme I
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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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UniProt
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bound to
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deduced amino acid sequence shows 6 hydrophobic transmembrane regions
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K4FKJ1_9ROSI
295
0
33653
TrEMBL
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232000
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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
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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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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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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
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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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partial purification of isoenzyme PI and isoenzyme PII
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expression in Escherichia coli
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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
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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
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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
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