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
3.1.1.31
-
RECOMMENDED NAME
GeneOntology No.
6-phosphogluconolactonase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
show the reaction diagram
first order reaction
-
6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
show the reaction diagram
PfGluPho functions on the basis of a rapid equilibrium random Bi Bi mechanism, where the binding of the second substrate depends on the first substrate
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
Q385D6
-
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
formaldehyde oxidation I
-
-
heterolactic fermentation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Pentose phosphate pathway
-
-
pentose phosphate pathway
-
-
pentose phosphate pathway (oxidative branch)
-
-
superpathway of glycolysis and Entner-Doudoroff
-
-
SYSTEMATIC NAME
IUBMB Comments
6-phospho-D-glucono-1,5-lactone lactonohydrolase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6-PGL
-
-
-
-
6-phospho-D-glucose-delta-lactone hydrolase
-
-
-
-
6-phosphoglucono-gamma-lactonase
-
-
-
-
6-phosphogluconolactonase
Q84WW2, Q8LEV7, Q8LG70, Q9FIN1, Q9LMX8
-
6-phosphogluconolactonase
-
-
6-phosphogluconolactonase
O95336
-
6-phosphogluconolactonase
-
-
6-phosphogluconolactonase
-
-
6-phosphogluconolactonase
Q27741
-
6-phosphogluconolactonase
-
-
6-phosphogluconolactonase
Q9GRG6
-
6-phosphogluconolactonase 3
-
-
6-phosphonogluconolactonase
-
-
6PGL
-
-
-
-
6PGL
Q84WW2, Q8LEV7, Q8LG70, Q9FIN1, Q9LMX8
-
6PGL
-
-
6PGL
O95336
-
6PGL
-
-
6PGL-G6PDH
Q27741
-
G6PD-6PGL
-
-
Glc6PD-6PGL
-
-
glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase
-
-
glucose-6-phosphate dehydrognease-6-phosphogluconolactonase
-
-
lactonase, phosphoglucono-
-
-
-
-
Pf6PGL
Q27741
-
PGL
-
-
-
-
PGL
Q9X2N2
pgl is a mmember of the hex regulon
phosphogluconolactonase
-
-
-
-
YbhE protein
-
-
CAS REGISTRY NUMBER
COMMENTARY
37278-45-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DF 2000; DF40, mutant of K-10; K-10, wild-type
-
-
Manually annotated by BRENDA team
DF40, mutant of K-10; K-10, wild-type
-
-
Manually annotated by BRENDA team
strain K-12
-
-
Manually annotated by BRENDA team
Escherichia coli DF 2000
DF 2000
-
-
Manually annotated by BRENDA team
Escherichia coli K-10
K-10, wild-type
-
-
Manually annotated by BRENDA team
10403S or 10403S mdrM deletion mutant (DP-L5444) background
-
-
Manually annotated by BRENDA team
bifunctional enzyme having also ec 1.1.1.49, i.e. glucose 6-phosphate dehydrogenase, activity
-
-
Manually annotated by BRENDA team
bifunctional enzyme having both glucose-6-phosphate dehydrogenase and 6-phosphogluconolactonase activity
SwissProt
Manually annotated by BRENDA team
strains PAO-S1 and PAO-B1
-
-
Manually annotated by BRENDA team
male Wistar
-
-
Manually annotated by BRENDA team
dried bakers yeast
-
-
Manually annotated by BRENDA team
wild-type MC3
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae MC3
wild-type MC3
-
-
Manually annotated by BRENDA team
MIT at 1.1, formerly designated 427-12/ICI-060, procyclic and bloodstream forms
-
-
Manually annotated by BRENDA team
Xanthomonas oryzae pv. oryzae
-
-
Manually annotated by BRENDA team
ATCC 31821 strain ZM4
-
-
Manually annotated by BRENDA team
Zymomonas mobilis ATCC 31821
ATCC 31821 strain ZM4
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
pgl deletion mutant has decreased growth in glucose-limiting minimal medium but grows normally when excess glucose is added. The Pgl deletion mutant has increased expression of several beta-glucosidases, consistent with inhibition of beta-glucosidases by 6-phosphogluconolactone, it accumulates and secretes a glucose-derived metabolite. Pgl deletion enhances activation of host IFN-beta expression independently of mdrM. At 48 h after infection of mice with 1 50% lethal dose, the pgl deletion mutant exhibits a 15- to 30fold growth defect in the liver and spleen. Pgl deletion mutant is more sensitive to oxidative stress, i.e., to diamide and hydrogen peroxide but not to the antibiotic control
malfunction
Q84WW2, Q8LEV7, Q8LG70, Q9FIN1, Q9LMX8
pgl3 mutation knocks out most of the 6PGL activity. Knockdown of PGL3 leads to a dramatic decrease in plant size, a significant increase in total glucose-6-phosphate dehydrogenase activity and a marked decrease in cellular redox potential. A wild-type PGL3-GFP transgene complements all phenotypes caused by the pgl3 mutation. Plastidic localization and enzymatic activity are required for PGL3 to complement the pgl3 mutant phenotypes. Pgl3 mutation exhibits constitutive pathogenesis-related gene expression and enhanced resistance to Pseudomonas syringae pv. maculicola ES4326 and Hyaloperonospora arabidopsidis Noco2. The pgl3 mutation activates NPR1- and SID2/EDS16/ICS1-dependent defense signaling
metabolism
-
in Plasmodium falciparum, glucose-6-phosphate dehydrogenase is combined with the second enzyme of the pentose phosphate pathway to create a unique bifunctional enzyme named GluPho, glucose-6-phosphate dehydrogenase/6-phosphogluconolactonase. The G6PD activity is not largely influenced by the 6PGL part
physiological function
Q84WW2, Q8LEV7, Q8LG70, Q9FIN1, Q9LMX8
PGL1 is dispensable for plant growth and development
physiological function
Q84WW2, Q8LEV7, Q8LG70, Q9FIN1, Q9LMX8
PGL2 is dispensable for plant growth and development
physiological function
Q84WW2, Q8LEV7, Q8LG70, Q9FIN1, Q9LMX8
PGL3 is the major contributor to total 6PGL activity. PGL3 is essential for plant growth and development. Plastidic localization and 6PGL activity of the PGL3 protein are essential for complementing all pgl3 phenotypes, indicating that the oxidative section of the plastidic pentose phosphate pathway is required for plant normal growth and development. PGL3 may function downstream of salicylic acid
physiological function
Q84WW2, Q8LEV7, Q8LG70, Q9FIN1, Q9LMX8
PGL5 is dispensable for plant growth and development
physiological function
-
the enzyme plays a key role during infection, by providing the important reductive agent NADPH, and forms ribose 5-phosphate, a major nucleic acid precursor, as well as several metabolic intermediates, such as fructose 6-phosphate and glyceraldehyde 3-phosphate
metabolism
-
the enzyme is one of the six enzymes of the pentose phosphate pathway of Trypanosoma brucei and hydrolyzes D-6-phosphogluconolactone to 6-phosphogluconic acid
additional information
-
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)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-5-oxo-2-tetrahydrofurancarboxylic acid + H2O
L-alpha-hydroxyglutaric acid
show the reaction diagram
-
-
-
-
?
6-phospho-D-glucono-1,4-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
the gamma-lactone is more stable than the natural delta-lactone substrate. It contains a five-membered heterocyclic ring, whereas the delta-lactone contains a six-membered heterocyclic ring
-
-
?
6-phospho-D-glucono-1,5-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
-
-
-
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
-
-
ir
6-phospho-D-glucono-1,5-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
-
-
-
?
6-phospho-D-glucono-1,5-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
-
-
-
?
6-phospho-D-glucono-1,5-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
-
-
-
ir
6-phospho-D-glucono-1,5-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
-
-
-
-
?
6-phospho-D-glucono-1,5-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
-
-
-
-
?
6-phospho-D-glucono-1,5-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
-
-
-
?
6-phospho-D-glucono-1,5-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
-
-
-
-
6-phospho-D-glucono-1,5-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
-
-
-
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
Q9X2N2
-
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
Q9GRG6
-
-
?
6-phospho-D-glucono-1,5-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
O95336
-
-
?
6-phospho-D-glucono-1,5-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
Q27741
-
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
6-phosphoglucono-delta-lactone is unstable and hydrolyzes spontaneously to the open-chain 6-phosphogluconate
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
6-phosphogluconolactone
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
6-phosphogluconolactone
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
6-phosphogluconolactone
-
ir
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
6-phosphogluconolactone
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
enzyme hydrolyzes both, the delta- and - gamma forms of 6-phosphogluconolactone
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
6-phospho-D-gluconate
-
ir
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
6-phospho-D-gluconate
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
6-phospho-D-gluconate
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
6-phospho-D-gluconate
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
6-phospho-D-gluconate
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
6-phospho-D-gluconate
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
6-phospho-D-gluconate
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
second step in pentose phosphate pathway
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
second step in pentose phosphate pathway
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
H165 is the catalytic residue, while R77 and R200 bind to the phosphate group. Ring opening of the lactone involves proton transfer from HE2 of H165 to O1 or O5 of the lactone, via a water molecule
-
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
Escherichia coli DF 2000
-
-
-
ir
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
Zymomonas mobilis ATCC 31821
-
6-phosphoglucono-delta-lactone is unstable and hydrolyzes spontaneously to the open-chain 6-phosphogluconate
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
Saccharomyces cerevisiae MC3
-
6-phosphogluconolactone
-
ir
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
Escherichia coli K-10
-
6-phospho-D-gluconate
-
ir
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
Escherichia coli K-10
-
-
-
ir
D-glucono-delta-lactone + H2O
?
show the reaction diagram
-
-
-
-
?
delta-6 phosphogluconolactone + H2O
6-phosphogluconic acid
show the reaction diagram
Q385D6
-
-
-
?
additional information
?
-
-
independence of glycolytic and pentose cycle intermediates in ad libitum fed rats
-
-
-
additional information
?
-
-
induction of 6-phosphogluconolactonase, phosphogluconate dehydrogenase and gluconokinase, enzymes of the oxidative pentose phosphate pathway by glucono-delta-lactone
-
-
-
additional information
?
-
-
the enzyme is involved in the second step of the pentose phosphate pathway
-
-
-
additional information
?
-
Saccharomyces cerevisiae MC3
-
induction of 6-phosphogluconolactonase, phosphogluconate dehydrogenase and gluconokinase, enzymes of the oxidative pentose phosphate pathway by glucono-delta-lactone
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
?
6-phospho-D-glucono-1,5-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
-
-
-
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
Q9X2N2
-
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
Q9GRG6
-
-
?
6-phospho-D-glucono-1,5-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
O95336
-
-
?
6-phospho-D-glucono-1,5-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
Q27741
-
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
second step in pentose phosphate pathway
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
-
second step in pentose phosphate pathway
-
?
delta-6 phosphogluconolactone + H2O
6-phosphogluconic acid
show the reaction diagram
Q385D6
-
-
-
?
additional information
?
-
-
independence of glycolytic and pentose cycle intermediates in ad libitum fed rats
-
-
-
additional information
?
-
-
induction of 6-phosphogluconolactonase, phosphogluconate dehydrogenase and gluconokinase, enzymes of the oxidative pentose phosphate pathway by glucono-delta-lactone
-
-
-
additional information
?
-
-
the enzyme is involved in the second step of the pentose phosphate pathway
-
-
-
additional information
?
-
Saccharomyces cerevisiae MC3
-
induction of 6-phosphogluconolactonase, phosphogluconate dehydrogenase and gluconokinase, enzymes of the oxidative pentose phosphate pathway by glucono-delta-lactone
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn
Q385D6
each monomer binds one Zn-atom, far away from catalytic site, plays structural role
Zn2+
-
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
LITERATURE
IMAGE
(NH4)2SO4
-
0.06 M, 55% inhibition
glucose-6-phosphate
-
competitive
glutathione
-
PfGluPho is inhibited by S-glutathionylation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
6-phospho-D-glucono-1,5-lactone
-
in situ
0.09
6-phospho-D-glucono-1,5-lactone
-
in situ
0.7
6-phospho-D-glucono-1,5-lactone
-
synthetic 6-phosphogluconolactone, pH 6.5
0.83
6-phospho-D-glucono-1,5-lactone
-
synthetic 6-phosphogluconolactone, pH 7.4
additional information
additional information
-
detailed kinetic analysis of the bifunctional glucose-6-phosphate dehydrogenase/6-phosphogluconolactonase indicates that PfGluPho functions on the basis of a rapid equilibrium random Bi Bi mechanism, where the binding of the second substrate depends on the first substrate
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1
-
recombinant Glc6PD-6PGL
1.18
-
-
46
-
recombinant PfGluPho, substrate is 6-phosphoglucono-gamma-lactone, pH 7.0, 25C
54.2
-
recombinant 6PGL
55.2
-
-
60
Q27741
recombinant 6PGL
60
-
recombinant PfGluPho, substrate is 6-phosphoglucono-delta-lactone, pH 7.0, 25C
180
-
recombinant 6PGL
1065
-
recombinant h6PGL, substrate is 6-phospho-D-glucono-1,5-lactone, pH 7.0, 25C
3330
-
recombinant 6PGL
additional information
-
specific activity in both cultured procyclic and bloodstream forms
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
enzyme activity in lymphocytes, monocytes, granulocytes and platelets is 10 times as high as that in erythrocytes, activity is independent of red cell age
additional information
-
-
additional information
-
specific activity is high in adipose tissue
additional information
-
-
additional information
-
spectrometric assay of the enzyme activity involving the use of immobilized enzymes to prepare the labile 6-phosphoglucono-delta-lactone substrate
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8
-
-
6 - 7.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8.2
-
approx. 40% of maximal activity at pH 5.2, approx. 20% of maximal activity at pH 8.2
5.7 - 8.5
-
approx. 50% of maximal activity at pH 5.8, approx. 60% of maximal activity at pH 8.0
5.8 - 7.5
-
spontaneous hydrolysis of 6-phospho-D-glucono-1,5-lactone
5.8 - 7.5
-
pH 8, spontaneous hydrolysis drastic increases above
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at
25
-
pH 7.0 provides favourable conditions for the enzyme assay
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q84WW2, Q8LEV7, Q8LG70, Q9FIN1, Q9LMX8
-
Manually annotated by BRENDA team
-
co-localization with thioredoxin m-type, Trx_m2
Manually annotated by BRENDA team
-
85% in bloodstream form of trypanosome
Manually annotated by BRENDA team
-
15% in bloodstream form of trypanosome
Manually annotated by BRENDA team
-
co-localization with thioredoxin m-type, Trx_m2
Manually annotated by BRENDA team
-
bifuntional enzyme having also hexose-6-phosphate dehydrogenase activity, distinct from cytosolic 6-phosphogluconolactonase
-
Manually annotated by BRENDA team
additional information
-
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
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768)
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
LITERATURE
25000
-
gel filtration
80871
25880
-
estimated from SDS-PAGE
690248
29000
-
gel filtration
80877
30000
Q385D6
-
675433
30000
-
native enzyme, gel filtration
80874
40000
-
SDS-PAGE
694040
60000
-
gel filtration
649488
107000
-
one subunit, determined by size exclusion chromatography
673539
178000
-
gel filtration
649488
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 110000, SDS-PAGE
dimer
-
2 * 89000, SDS-PAGE
monomer
-
1 * 30000, SDS-PAGE
monomer
-
1 * 30000, SDS-PAGE
monomer
-
1 * 26000, SDS-PAGE
monomer
-
1 * 27529, calculation from sequence of amino acids
monomer
-
1* 25880, estimated from SDS-PAGE
monomer
Zymomonas mobilis ATCC 31821
-
1 * 26000, SDS-PAGE
-
tetramer
-
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
-
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
Q385D6
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
44% loss of activity after 5 min; 95% loss of 6PGL activity after 5 min
649488
60
-
5 min, 30% loss of activity
80869
65
-
5 min, complete loss of activity
80869
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
22C, enzyme activity in erythrocytes is stable for 6 days stored in citrate dextrose, heparin and EDTA as anticoagulants
-
4C, enzyme activity in erythrocytes is stable for 20 days stored in citrate dextrose, heparin and EDTA as anticoagulants
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-tagged YbhE protein
-
recombinant 6PGL
-
2',5'-ADP-Sepharose
-
recombinant G6PD-6PGL
-
recombinant Glc6PD-6PGL
-
recombinant 6PGL
Q27741
His-Trap nickel affinity column chromatography and Superdex 75 gel filtration
-
purified to 95% homogeneity in a single step with a Co-NTA column
Q385D6
recombinant 6PGL
Q9GRG6
to 95% homogeneity in a single step with an NTA column
-
Ni-NTA His-Bind resin chromatography and UNO6 Q column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
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
Q84WW2, Q8LEV7, Q8LG70, Q9FIN1, Q9LMX8
expression in Escherichia coli
-
gene h6PGL, overexpression as N-terminally His-tagged enzyme in Escherichia coli strain BL21 using vector pRAREII
-
wild-type or pgl mutant expressed in mice
-
expression in Escherichia coli
-
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
-
expression of lactonase domain Pf6PGL in Escherichia coli, low recovery of soluble Pf6PGL
Q27741
expressed as a His fusion protein in Escherichia coli BL21(DE3) cells
-
pgl is a member of the hex regulon
Q9X2N2
expression in Escherichia coli
Q9GRG6
expressed in Escherichia coli BL21 (DE3) cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D150A
Q84WW2, Q8LEV7, Q8LG70, Q9FIN1, Q9LMX8
displays pgl3 morphology, does not complement the pgl3 phenotypes
D150A/D231A/H233A
Q84WW2, Q8LEV7, Q8LG70, Q9FIN1, Q9LMX8
displays pgl3 morphology, does not complement the pgl3 phenotypes
D231A/H233A
Q84WW2, Q8LEV7, Q8LG70, Q9FIN1, Q9LMX8
displays pgl3 morphology, does not complement the pgl3 phenotypes
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
the enzyme is a target for anti-parasite drug development