Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ADP + H2O
?
-
103% relative activity
-
-
?
AMP + H2O
?
-
5% relative activity
-
-
?
ATP + H2O
?
-
41% relative activity
-
-
?
Ca-phytate + H2O
?
-
133% relative activity
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8, 3.1.3.26, and 3.1.3.72
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
Na-phytate + H2O
?
-
100% relative activity
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
phenyl phosphate + H2O
?
-
32% relative activity
-
-
?
additional information
?
-
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
hydrolysis of the phosphate ester at the D-5 position
symmetrical product, only isomer of IP5 as product
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
high substrate specificity for phytic acid
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
high substrate specificity for phytic acid
symmetrical product, only isomer of IP5 as product
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
myo-inositol-1,2,3,4,5,6-hexakisphosphate is identical with phytic acid
symmetrical product, only isomer of IP5 as product
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
enzyme activity may be regulated by the intracellular Ca2+ concentration
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
important component of phytic acid metabolism, constitutive enzyme
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
phytic acid is a major component of seeds and pollen grains, localized in membrane-bound phytic-rich granules
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
myo-inositol-1,2,3,4,5,6-hexakisphosphate is identical with phytic acid
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
myo-inositol-1,2,3,4,5,6-hexakisphosphate is identical with phytic acid
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
myo-inositol-1,2,3,4,5,6-hexakisphosphate is identical with phytic acid
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
5% relative activity
-
-
?
additional information
?
-
-
myo-inositol pentakisphosphates are no good substrates, terminal hydrolysis to myo-inositol trisphosphate
-
-
?
additional information
?
-
-
two subsequent dephosphorylations occur adjacent to the D-5 hydroxyl group to yield myo-inositol-1,2,3-trikisphosphate as the final product, rates of removal of the second and third phosphates are significantly lower, possibly due to reduced specificity for IP5 and IP4 and inhibition by the phosphate released, IP4: only one isomer, either I-1,2,3,4-P4 or its enantiomer I-1,2,3,6-P4, no further hydrolysis of IP3
-
-
?
additional information
?
-
the tyrosine phosphatase (PTP)-like inositol polyphosphatase from Selenomonas ruminantium subsp. lactilytica dephosphorylates myo-inositol hexakisphosphate (Ins P(6)) in vitro preferentially cleaving the 5-phosphate position. Enzyme PhyAsrl has a general specificity for polyphosphorylated myo-inositol substrates, but can also dephosphorylate molecules containing high energy diphosphate bonds in vitro. It can produce Ins(2)P via a highly unique and ordered pathway of sequential dephosphorylation: Ins P(6), Ins(1,2,3,4,6)P(5), D-Ins(1,2,3,6)P(4), Ins(1,2,3)P(3), and D/L-Ins(1,2)P(2)
-
-
?
additional information
?
-
-
the tyrosine phosphatase (PTP)-like inositol polyphosphatase from Selenomonas ruminantium subsp. lactilytica dephosphorylates myo-inositol hexakisphosphate (Ins P(6)) in vitro preferentially cleaving the 5-phosphate position. Enzyme PhyAsrl has a general specificity for polyphosphorylated myo-inositol substrates, but can also dephosphorylate molecules containing high energy diphosphate bonds in vitro. It can produce Ins(2)P via a highly unique and ordered pathway of sequential dephosphorylation: Ins P(6), Ins(1,2,3,4,6)P(5), D-Ins(1,2,3,6)P(4), Ins(1,2,3)P(3), and D/L-Ins(1,2)P(2)
-
-
?
additional information
?
-
the enzyme shows no or poor activity with ATP, ADP, 4-nitrophenyl phosphate, diphosphate, glucose 6-phosphate, and fructose 6-phosphate
-
-
?
additional information
?
-
-
no activity with riboflurin phosphate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8, 3.1.3.26, and 3.1.3.72
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
enzyme activity may be regulated by the intracellular Ca2+ concentration
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
important component of phytic acid metabolism, constitutive enzyme
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
phytic acid is a major component of seeds and pollen grains, localized in membrane-bound phytic-rich granules
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Scott, J.J.; Loewus, F.A.
A calcium-activated phytase from pollen of Lilium longiflorum
Plant Physiol.
82
333-335
1986
Lilium longiflorum
brenda
Baldi, B.G.; Scott, J.J.; Everard, J.D.; Loewus, F.A.
Localization of constitutive phytases in lily pollen and properties of the pH 8 form
Plant Sci.
56
137-147
1988
Lilium longiflorum, Pinus ponderosa, Typha latifolia
-
brenda
Barrientos, L.; Scott, J.J.; Murthy, P.P.N.
Specificity of hydrolysis of phytic acid by alkaline phytase from lily pollen
Plant Physiol.
106
1489-1495
1994
Lilium longiflorum
brenda
Scott, J.J.
Alkaline phytase activity in nonionic detergent extracts of legume seeds
Plant Physiol.
95
1298-1301
1991
Medicago sativa, Phaseolus vulgaris, Pisum sativum
brenda
Jog, S.P.; Garchow, B.G.; Mehta, B.D.; Murthy, P.P.N.
Alkaline phytase from lily pollen: Investigation of biochemical properties
Arch. Biochem. Biophys.
440
133-140
2005
Lilium longiflorum
brenda
Gulati, H.K.; Chadha, B.S.; Saini, H.S.
Production and characterization of thermostable alkaline phytase from Bacillus laevolacticus isolated from rhizosphere soil
J. Ind. Microbiol. Biotechnol.
34
91-98
2007
Sporolactobacillus laevolacticus
brenda
Garchow, B.G.; Jog, S.P.; Mehta, B.D.; Monosso, J.M.; Murthy, P.P.
Alkaline phytase from Lilium longiflorum: Purification and structural characterization
Protein Expr. Purif.
46
221-232
2006
Lilium longiflorum
brenda
Yang, M.; Johnson, S.C.; Murthy, P.P.
Enhancement of alkaline phytase production in Pichia pastoris: influence of gene dosage, sequence optimization and expression temperature
Protein Expr. Purif.
84
247-254
2012
Lilium longiflorum (Q0GYS2)
brenda
Yang, M.; Teymorian, S.; Olivares, P.; Murthy, P.
Extracellular expression of alkaline phytase in Pichia pastoris Influence of signal peptides, promoters and growth medium
Biotechnol. Rep.
6
112-118
2015
Lilium longiflorum (Q0GYS2)
brenda
Puhl, A.A.; Greiner, R.; Selinger, L.B.
A protein tyrosine phosphatase-like inositol polyphosphatase from Selenomonas ruminantium subsp. lactilytica has specificity for the 5-phosphate of myo-inositol hexakisphosphate
Int. J. Biochem. Cell Biol.
40
2053-2064
2008
Selenomonas ruminantium subsp. lactilytica (Q0ZQJ3), Selenomonas ruminantium subsp. lactilytica
brenda
Pal Roy, M.; Mazumdar, D.; Dutta, S.; Saha, S.P.; Ghosh, S.
Cloning and expression of phytase appA gene from Shigella sp. CD2 in Pichia pastoris and comparison of properties with recombinant enzyme expressed in E. coli
PLoS ONE
11
e0145745
2016
Shigella sp. CD2 (F6IQ86)
brenda