Information on EC 3.1.3.23 - sugar-phosphatase

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

EC NUMBER
COMMENTARY hide
3.1.3.23
-
RECOMMENDED NAME
GeneOntology No.
sugar-phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sugar phosphate + H2O = sugar + phosphate
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
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SYSTEMATIC NAME
IUBMB Comments
sugar-phosphate phosphohydrolase
Has a wide specificity, acting on aldohexose 1-phosphates, ketohexose 1-phosphates, aldohexose 6-phosphates, ketohexose 6-phosphates, both phosphate ester bonds of fructose 1,6-bisphosphate, phosphoric esters of disaccharides, and on pentose and triose phosphates, but at a slower rate.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-07-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
araL gene
-
-
Manually annotated by BRENDA team
sugar phosphate phosphatase II
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-
Manually annotated by BRENDA team
Escherichia acidilactici
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-
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Manually annotated by BRENDA team
sugar phosphate phosphatase II
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-
Manually annotated by BRENDA team
sugar phosphate phosphatase I and sugar phosphate phosphatase II
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-
Manually annotated by BRENDA team
sugar phosphate phosphatase II
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
loss of HAD1 is required for fosmidomycin resistance. Parasites lacking HAD1 have increased methylerythritol phosphate pathway metabolites, particularly the deoxyxylulose 5-phosphate reductoisomerase substrate deoxyxylulose 5-phosphate
metabolism
physiological function
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putative physiological role of the enzyme AraL in the detoxification of accidental accumulation of phosphorylated metabolites
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-diphosphoglycerate + H2O
?
show the reaction diagram
-
-
-
-
?
2-Deoxy-D-glucose 6-phosphate + H2O
2-Deoxy-D-glucose + phosphate
show the reaction diagram
2-deoxy-D-ribose 5-phosphate + H2O
2-deoxy-D-ribose + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
alpha-cellobiose 1-phosphate + H2O
alpha-cellobiose + phosphate
show the reaction diagram
-
-
-
-
?
alpha-D-galactose 1-phosphate + H2O
alpha-D-galactose + phosphate
show the reaction diagram
alpha-D-gentibiose-1-phosphate + H2O
alpha-D-gentibiose + phosphate
show the reaction diagram
-
66% of the activity with alpha-D-glucose 1-phosphate
-
-
?
alpha-D-glucosamine 1-phosphate + H2O
alpha-D-glucosamine + phosphate
show the reaction diagram
-
-
-
-
?
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
show the reaction diagram
alpha-D-glucuronic acid 1-phosphate + H2O
alpha-D-glucuronic acid + phosphate
show the reaction diagram
alpha-D-mannose 1-phosphate + H2O
alpha-D-mannose + phosphate
show the reaction diagram
alpha-gentiobiose 1-phosphate + H2O
alpha-gentiobiose + phosphate
show the reaction diagram
-
-
-
-
?
alpha-lactose 1-phosphate + H2O
alpha-lactose + phosphate
show the reaction diagram
alpha-maltose 1-phosphate + H2O
alpha-maltose + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-methyl-thiogalactopyranoside 6-phosphate + H2O
beta-D-methyl-thiogalactopyranoside + phosphate
show the reaction diagram
-
-
-
-
?
D-arabinose 5-phosphate + H2O
D-arabinose + phosphate
show the reaction diagram
-
-
-
-
?
D-erythrose 4-phosphate + H2O
D-erythrose + phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-fructose 1,6-diphosphate + H2O
?
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
D-galactose 1-phosphate + H2O
D-galactose + phosphate
show the reaction diagram
-
-
-
-
?
D-galactose 6-phosphate + H2O
D-galactose + phosphate
show the reaction diagram
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
?
D-glucose 2-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
second best substrate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
D-glyceraldehyde 3-phosphate + H2O
D-glyceraldehyde + phosphate
show the reaction diagram
-
24.5% of the activity with alpha-D-glucose 1-phosphate
-
-
?
D-mannose 6-phosphate + H2O
D-mannose + phosphate
show the reaction diagram
D-ribose 5-phosphate + H2O
D-ribose + phosphate
show the reaction diagram
D-ribulose 5-phosphate + H2O
D-ribulose + phosphate
show the reaction diagram
-
-
-
?
D-sorbose 1,6-diphosphate + H2O
?
show the reaction diagram
-
15% of the activity with alpha-D-glucose 1-phosphate
-
-
?
D-sorbose 1-phosphate + H2O
D-sorbose + phosphate
show the reaction diagram
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108% of the activity with alpha-D-glucose 1-phosphate
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-
?
D-xylose 1-phosphate + H2O
D-xylose + phosphate
show the reaction diagram
D-xylulose 5-phosphate + H2O
D-xylulose + phosphate
show the reaction diagram
-
-
-
-
?
deoxyribose 5-phosphate + H2O
deoxyribose + phosphate
show the reaction diagram
-
-
-
?
deoxyxylulose 5-phosphate + H2O
deoxyxylulose + phosphate
show the reaction diagram
-
-
-
?
dihydroxyacetone phosphate + H2O
dihydroxyacetone + phosphate
show the reaction diagram
DL-glycerol 3-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
?
inositol phosphate + H2O
inositol + phosphate
show the reaction diagram
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5% of the activity with alpha-D-glucose 1-phosphate
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-
?
mannitol 1-phosphate + H2O
mannitol + phosphate
show the reaction diagram
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-
-
-
?
methylerythritol phosphate + H2O
methylerythritol + phosphate
show the reaction diagram
-
-
-
?
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-fructose 1-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
Q8IJ74
best substrate
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-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
stimulates to a lesser degree than Mg2+
Fe2+
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stimulates to a lesser degree than Mg2+
Mn2+
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stimulates to a lesser degree than Mg2+
Zn2+
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stimulates to a lesser degree than Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dodecyl sulfate
F-
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10 mM, 98% inhibition of hydrolysis of glucose 6-phosphate, 70% inhibition of hydrolysis of glucose 1-phosphate
glucose 1-phosphate
guanidine
mannose 1-phosphate
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strong competitive inhibitor of hydrolysis of glucose 6-phosphate
p-mercuribenzoate
additional information
-
no inhibition by 5-fluorouracil
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S46D HPr
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.1 - 5.9
2-deoxy-D-glucose 6-phosphate
50
4-nitrophenyl phosphate
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pH 7.0, 37C
2.5
alpha-D-galactose 1-phosphate
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2.2
alpha-D-gentiobiose 1-phosphate
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2.5
alpha-D-glucose 1-phosphate
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2.3
alpha-D-lactose 1-phosphate
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2.2
alpha-D-maltose 1-phosphate
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2.5 - 3
alpha-D-mannose 1-phosphate
2.1
alpha-D-xylose 1-phosphate
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-
27.36
D-arabinose 5-phosphate
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pH 7.0, 37C
40.78
D-fructose 1,6-bisphosphate
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pH 7.0, 37C
2.8
D-Fructose 1-phosphate
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3 - 34.89
D-fructose 6-phosphate
40.74
D-galactose 1-phosphate
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pH 7.0, 37C
3.1
D-galactose 6-phosphate
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3
D-glucosamine 6-phosphate
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3.1 - 24.96
D-glucose 6-phosphate
1.2
D-glucuronate 1-phosphate
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4.9 - 6.7
D-mannose 6-phosphate
3.3 - 5.9
D-ribose 5-phosphate
29.14
D-xylulose 5-phosphate
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pH 7.0, 37C
7.1 - 8.3
DL-glycerol 3-phosphate
50
mannitol 1-phosphate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
31 - 34
2-deoxy-D-glucose 6-phosphate
0.012
4-nitrophenyl phosphate
-
pH 7.0, 37C
2.92
D-arabinose 5-phosphate
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pH 7.0, 37C
1.49
D-fructose 1,6-bisphosphate
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pH 7.0, 37C
2.817 - 19
D-fructose 6-phosphate
4.28
D-galactose 1-phosphate
-
pH 7.0, 37C
2.49 - 26
D-glucose 6-phosphate
26 - 33
D-mannose 6-phosphate
33 - 39
D-ribose 5-phosphate
2.75
D-xylulose 5-phosphate
-
pH 7.0, 37C
6.6 - 24
DL-glycerol 3-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.2 - 7.2
2-deoxy-D-glucose 6-phosphate
0.00024
4-nitrophenyl phosphate
-
pH 7.0, 37C
0.106
D-arabinose 5-phosphate
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pH 7.0, 37C
0.0365
D-fructose 1,6-bisphosphate
-
pH 7.0, 37C
0.0807 - 2.5
D-fructose 6-phosphate
0.102
D-galactose 1-phosphate
-
pH 7.0, 37C
0.0998 - 3.8
D-glucose 6-phosphate
3.8 - 6.7
D-mannose 6-phosphate
5.6 - 10.7
D-ribose 5-phosphate
0.0943
D-xylulose 5-phosphate
-
pH 7.0, 37C
0.8 - 3.4
DL-glycerol 3-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.52
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strain C
11.42
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var. communior
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9
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hydrolysis of glucose 1-phosphate or glucose 6-phosphate
7 - 8
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hydrolysis of mannitol 1-phosphate, with or without the activator S46D HPr
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9
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although, at pH 8 and pH 9, the enzyme activity is considerably lower than at pH 7.0, the values are higher than at pH 6.0, no activity below pH 4.0, profile, overview
4 - 8
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pH 4.0: about 55% of maximal activity, pH 8.0: about 45% of maximal activity, hydrolysis of glucose 1 -phosphate
5 - 9
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about 60% of maximal activity at pH 5.0 and at pH 9.0, hydrolysis of mannitol 1-phosphate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
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recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 70
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optimal activity at 37C, no activity at 25C, profile, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28900
-
x * 28900, about, sequence calculation
33000
x * 33000, SDS-PAGE
42700
x * 42700, maltose-binding protein-bound enzyme, SDS-PAGE
51000
-
2 * 51000, SDS-PAGE
97000
-
var. communior, gel filtration
98000
-
gel filtration
99000
Escherichia acidilactici
-
gel filtration
100000
101000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1M HEPES (pH 7.5) and 20-25% (w/v) PEG 8000
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9.7
-
30C, stable for at least 40 min
94723
4 - 9
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60C, 2 min, quite stable
94723
6
-
stable up to 55C. At 60C, 2 min, about 20% loss of activity. At 65C, 2 min, 80% loss of activity
94723
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
pH 3.0-9.7, stable for at least 40 min, not stable above pH 10 or below pH 2.5
55
-
pH 6, 2 min, stable up to
60
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pH 4.0-9.0, 2 min, quite stable. At pH 6.0, 20% loss of activity after 2 min. Complete loss of activity at pH 1.0, 2.0, 3.0 or 10.0 after 2 min
65
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pH 6.0, 2 min, 80% loss of activity
100
-
10 min, unaffected
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
1-3C, pH 10, stable for 12 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amylose resin column chromatography
nickel agarose bead chromatography and Superdex 200 gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 95% homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
araL gene, the fourth cistron of the transcriptional unit araABDLMNPQ-abfA, DNA and amino acid sequence determination and analysis, overexpression of the His-tagged enzyme in Escherichia coli
-
expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli TB1 cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A69M
the mutation slightly affects the substrate specificity
H72K
the mutant is inactive in phosphomonoester dephosphorylation
I68M
the mutation slightly affects the substrate specificity
I68M/A69M/K71R/H72K
the mutant is inactive in phosphomonoester dephosphorylation
K71R
the mutation slightly affects the substrate specificity
G12D
-
strain IQB849 carrying a single-base substitution C to A introduced in the hairpin region displaying an augment in araL'-'lacZ expression of about 30fold in the presence of inducer, the point mutation increases the free energy of the mRNA secondary structure
T9K/G12D
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the double point mutation, C to A and G to T, introduced a compensatory T in the other part of the stem, thus regenerating the stem-loop structure in strain IQB857 and drastically reducing the expression of araL'-'lacZ
N70S
the mutant shows wild type activity
additional information
-
a translational fusion of the 5'-end of the araL gene to the lacZ reporter gene from Escherichia coli is constructed and integrated into the Bacillus subtilis chromosome. The construct comprises the araL ribosome-binding site, the initiation codon and a fusion between codon 10 of araL and codon 7 of Escherichia coli lacZ
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