Information on EC 3.1.3.22 - mannitol-1-phosphatase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.1.3.22
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RECOMMENDED NAME
GeneOntology No.
mannitol-1-phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-mannitol 1-phosphate + H2O = D-mannitol + phosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mannitol biosynthesis
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mannitol cycle
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Fructose and mannose metabolism
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SYSTEMATIC NAME
IUBMB Comments
D-mannitol-1-phosphate phosphohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9055-29-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
marine red algae from estuarine areas
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Manually annotated by BRENDA team
Ceratocystis multiannulata
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Manually annotated by BRENDA team
phaeophycean alga
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
phaeophycean alga
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
no activity in Agaricus bisporus
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Manually annotated by BRENDA team
no activity in Fomes pinicola
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Manually annotated by BRENDA team
no activity in Mucor lusitanicus
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-
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Manually annotated by BRENDA team
no activity in Phycomyces blakesleeanus
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Manually annotated by BRENDA team
no activity in Polyporus versicolor
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Manually annotated by BRENDA team
no activity in Rhizopus arrhizus
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Manually annotated by BRENDA team
Penicillus frequentans
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Manually annotated by BRENDA team
Platymonas suecica
prasinophycean alga
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Manually annotated by BRENDA team
Spatoglossum sp.
phaeophycean alga
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
D-fructose 1-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
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1.8% of the activity with D-mannitol 1-phosphate
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?
D-mannitol 1-phosphate + H2O
D-mannitol + phosphate
show the reaction diagram
mannitol 1-phosphate + H2O
mannitol + phosphate
show the reaction diagram
sorbitol 1-phosphate + H2O
sorbose + phosphate
show the reaction diagram
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2.3% of the activity with D-mannitol 1-phosphate
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?
additional information
?
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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
D-mannitol 1-phosphate + H2O
D-mannitol + phosphate
show the reaction diagram
mannitol 1-phosphate + H2O
mannitol + phosphate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
activates the phosphatase activity, 14% activation compared to Mg2+; stimulates activity but not as efficient as Mg2+
Cu2+
activates phosphatase activity, 15% activation compared to Mg2+; stimulates activity but not as efficient as Mg2+
Fe2+
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2.5 fold activation
Mn2+
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2 fold activation
Zn2+
activates the phosphatase activity, 30% activation compared to Mg2+; stimulates activity but not as efficient as Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxymercuribenzoate
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complete inhibtion at 1 mM
ammonium sulfate
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complete inactivation with higher concentrations
Ca2+
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1 mM, 46% inhibition
diethyl dicarbonate
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at pH 6-8, due to histidine modification
mannitol
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inhibition of 50% or more
NaCN
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slightly inhibitory
NEM
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1 mM, complete inhibition, 79% inhibition at 0.1 mM
p-hydroxymercuribenzoate
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0.001 mM, complete inhibition
PCMB
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partially restored by addition of cysteine
Sodium fluoride
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.41 - 0.67
D-mannitol 1-phosphate
0.2 - 3
mannitol 1-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
D-mannitol 1-phosphate
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at pH 7.5 and 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02239
D-mannitol 1-phosphate
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at pH 7.5 and 30°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028
NaCl
Eimeria tenella
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inhibits native M1Pase with an IC50 value of 0.028 mM, for recombinant enzymes between 0.054 mM and 0.044 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.23
Ceratocystis multiannulata
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0.28
Penicillus frequentans
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103
enzyme in presence of 5 mM MgSO4, pH 6.5, 30°C
1792
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after ammonium sulfate fractionation
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
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7.9 - 8.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 6
the enzyme retains activity of 60% at pH 6.0 and 47% at pH 4.5, respectively
4.7 - 6
60% of maximal activity at pH 6.0 and 47% at pH 4.5
5.5 - 9
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6.5 - 8.5
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pH 6.5: about 60% of maximal activity, pH 8.5: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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unsporulated
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28500
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gel filtration
30200
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1 * 30200, SDS-PAGE
34650
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LC-ESI-MS analysis
34740
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calculation from sequence of cDNA
36000
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4 * 36000, calculated from amino acid sequence
155000
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isoform M1Pase2, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
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by cDNA in comparison to the biochemical purified enzyme, active side H82 phosphorylated, detected by diethyl pyrocarbonate inhibition and reduced inhibition by p-nitrophenylphosphate
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
rather unstable in presence of ammonium sulfate
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
biochemical purification of native enzyme; recombinant fusion and His-tagged proteins
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MnCl2 fractionation, ammonium sulfate precipitation
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Ni2+-affinity column chromatography
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ultracentrifugation and ammonium sulfate fractionation
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA from total RNA from unsporulated oocytes
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co-expression of the enzyme in construct with gene mtlD encoding the mannitol 1-phosphate dehydrogenase of Lactobacillus plantarum in a nisin-dependent overexpression system in different strains of Lactococcus lactis, subcloning in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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gene mtlD, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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optimization of co-expression of the enzyme in construct with gene mtlD encoding the mannitol 1-phosphate dehydrogenase of Lactobacillus plantarum in a nisin-dependent overexpression system in Lactococcus lactis resulting in increased D-mannitol production in Lactococcus lactis
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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the enzyme is a target for engineering to produce salt-tolerant transgenic horticultural crop plants
biotechnology
medicine
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lack of mannitol metabolism in higher eukaryotes