Information on EC 3.1.1.31 - 6-phosphogluconolactonase

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

EC NUMBER
COMMENTARY hide
3.1.1.31
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RECOMMENDED NAME
GeneOntology No.
6-phosphogluconolactonase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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formaldehyde oxidation I
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heterolactic fermentation
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Metabolic pathways
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Microbial metabolism in diverse environments
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pentose phosphate pathway
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Pentose phosphate pathway
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pentose phosphate pathway (oxidative branch)
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superpathway of glycolysis and Entner-Doudoroff
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SYSTEMATIC NAME
IUBMB Comments
6-phospho-D-glucono-1,5-lactone lactonohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
37278-45-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
DF 2000
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Manually annotated by BRENDA team
K-10, wild-type
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Manually annotated by BRENDA team
10403S or 10403S mdrM deletion mutant (DP-L5444) background
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
bifunctional enzyme having also ec 1.1.1.49, i.e. glucose 6-phosphate dehydrogenase, activity
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Manually annotated by BRENDA team
wild-type MC3
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Manually annotated by BRENDA team
Xanthomonas oryzae pv. oryzae
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Manually annotated by BRENDA team
ATCC 31821 strain ZM4
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Manually annotated by BRENDA team
Zymomonas mobilis ATCC 31821
ATCC 31821 strain ZM4
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
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analysis of effects of ligand binding on the internal dynamics of the enzyme by molecular dynamics simulations and nuclear magnetic resonance, alterations of conformational exchange, overview. Residues R77 and R200, located near the active site, interact directly with the phosphate group of 6-phospho-D-gluconate. Residue H165 is actively involved in catalysis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-5-oxo-2-tetrahydrofurancarboxylic acid + H2O
L-alpha-hydroxyglutaric acid
show the reaction diagram
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-
-
-
?
6-phospho-D-glucono-1,4-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
D-glucono-delta-lactone + H2O
?
show the reaction diagram
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?
delta-6 phosphogluconolactone + H2O
6-phosphogluconic acid
show the reaction diagram
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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
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
delta-6 phosphogluconolactone + H2O
6-phosphogluconic acid
show the reaction diagram
Q385D6
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn
each monomer binds one Zn-atom, far away from catalytic site, plays structural role
Zn2+
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has a structural role rather than a catalytic one, lies at the center of a tetrahedron. The side chains of H56 and H97 are at a distance of 2.0 A from the metal ion, while the oxygen atom of the carboxylic side chain of D98 coordinates the zinc ion in a monodentate manner. Water molecule at 2.7 A from the metal ion
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
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0.06 M, 55% inhibition
glucose-6-phosphate
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competitive
glutathione
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PfGluPho is inhibited by S-glutathionylation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 0.83
6-phospho-D-glucono-1,5-lactone
additional information
additional information
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1
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recombinant Glc6PD-6PGL
1.18
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46
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recombinant PfGluPho, substrate is 6-phosphoglucono-gamma-lactone, pH 7.0, 25C
54.2
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recombinant 6PGL
55.2
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180
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recombinant 6PGL
1065
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recombinant h6PGL, substrate is 6-phospho-D-glucono-1,5-lactone, pH 7.0, 25C
3330
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recombinant 6PGL
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8
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6 - 7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.2
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approx. 40% of maximal activity at pH 5.2, approx. 20% of maximal activity at pH 8.2
5.7 - 8.5
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approx. 50% of maximal activity at pH 5.8, approx. 60% of maximal activity at pH 8.0
5.8 - 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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co-localization with thioredoxin m-type, Trx_m2
Manually annotated by BRENDA team
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bifuntional enzyme having also hexose-6-phosphate dehydrogenase activity, distinct from cytosolic 6-phosphogluconolactonase
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Manually annotated by BRENDA team
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co-localization with thioredoxin m-type, Trx_m2
Manually annotated by BRENDA team
additional information
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PGL3 contains an N-terminal extension and a C-terminal peroxisome-targeting motif PTS1, subcellular localization of enzyme stages, overview. Besides redox-related and metabolic signals that influence dual-targeting of enzyme PGL3 in leaves, developmental and/or physiological state(s) play another role for subcellular enzyme localization in different plant parts, the metabolic state affects PGL3 targeting by absence/reduced stability of thioredoxin Trxm2
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Plasmodium vivax (strain Salvador I)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
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gel filtration
25880
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estimated from SDS-PAGE
29000
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gel filtration
40000
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SDS-PAGE
60000
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gel filtration
107000
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one subunit, determined by size exclusion chromatography
178000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 110000, SDS-PAGE
dimer
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2 * 89000, SDS-PAGE
monomer
tetramer
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4*107kDA
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by the hanging-drop method, 6PGL in complex with two ligands, 6-phosphogluconic acid and citrate, at 2.2 A and 2.0 A resolution, respectively. Structures of the two complexes and of the apo form are almost identical. Both complexes belong to space group P21 and have two molecules in the asymmetric unit, related by a pure translation. PGL in complex with 6-phosphogluconic acid has unit cell parameters of a = 49.66, b = 87, c= 64.91 A and beta = 96.43. PGL in complex with citrate has unit cell parameters of a = 49.46, b = 87.21, c= 64.79 A and beta = 96.53
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hanging-drop method, equilibrated against a reservoir solution of 100 mM Hepes (pH 7.5), 30% (v/v) PEG MME 2000, 50 mM sodium acetate
hanging drop vapour diffusion method, using 0.1 M Bis-Tris pH 5.5, 25% (w/v) PEG 3350, and 0.2 M ammonium acetate
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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44% loss of activity after 5 min; 95% loss of 6PGL activity after 5 min
60
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5 min, 30% loss of activity
65
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5 min, complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
22C, enzyme activity in erythrocytes is stable for 6 days stored in citrate dextrose, heparin and EDTA as anticoagulants
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4C, enzyme activity in erythrocytes is stable for 20 days stored in citrate dextrose, heparin and EDTA as anticoagulants
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2',5'-ADP-Sepharose
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His-tagged YbhE protein
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His-Trap nickel affinity column chromatography and Superdex 75 gel filtration
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Ni-NTA His-Bind resin chromatography and UNO6 Q column chromatography
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purified to 95% homogeneity in a single step with a Co-NTA column
recombinant 6PGL
recombinant G6PD-6PGL
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recombinant Glc6PD-6PGL
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to 95% homogeneity in a single step with an NTA column
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of the gene encoding PfGluPho from chromosome 14 of the 3D7 gametocyte cDNA library, heterologous overexpression of PfGluPho using vector pQE30 in Escherichia coli strain M15
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expressed as a His fusion protein in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21 (DE3) cells
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expression in Escherichia coli
expression of lactonase domain Pf6PGL in Escherichia coli, low recovery of soluble Pf6PGL
gene h6PGL, overexpression as N-terminally His-tagged enzyme in Escherichia coli strain BL21 using vector pRAREII
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gene PGL3, presence of the C-terminal SKL motif interfered with chloroplast import of a PGL3_N-full-CFP fusion and with that of a PGL3_long medial-CFP fusion (with free N- and C-terminal ends) exclusively labeling peroxisomes, co-expression of thioredoxin Trxm2 with C-terminally truncated enzyme PGL3_N-short and _N-long versions accumulate in the cytosol of tobacco protoplasts and co-localization with Trxm2 in the cytosol and in the chloroplast stroma, recombinant expression of N-terminally CFP-tagged, green-fluorescent enzyme in Nicotiana benthamiana leaves
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PCR product cloned into the corresponding sites of the vector pGEX-4T-1 and then introduced into Escherichia coli. Constructs (35S:DELTANTpgl3-GFP and 35S:pgl3 DELTASKL-GFP) together with the 35S:PGL3-GFP construct transformed into the pgl3 background. Escherichia coli cells expressing GST-PGL3 and GST-pgl3 mutants
pgl is a member of the hex regulon
wild-type or pgl mutant expressed in mice
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D150A
displays pgl3 morphology, does not complement the pgl3 phenotypes
D150A/D231A/H233A
displays pgl3 morphology, does not complement the pgl3 phenotypes
D231A/H233A
displays pgl3 morphology, does not complement the pgl3 phenotypes
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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the enzyme is a target for anti-parasite drug development
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