Information on EC 5.3.1.9 - Glucose-6-phosphate isomerase

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

EC NUMBER
COMMENTARY
5.3.1.9
-
RECOMMENDED NAME
GeneOntology No.
Glucose-6-phosphate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-Glucose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
push-pull mechanism of ring opening in which H388 breaks the O5-C1 bond by donating a proton, and simultaneously, K518 abstracts a proton from the C1 hydroxyl group
P06745
D-Glucose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
mechanism is based on an enediol intermediate
-
D-Glucose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
multistep catalytic mechanism, model including catalytically active amino acids
-
D-Glucose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
cis-endiol intermediate based mechanism with Glu97 acting as the catalytic base responsible for isomerization
-
D-Glucose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
on the basis of the calculations and simulations, a zwitterionic intermediate mechanism for the low-energy enzymatic reaction is proposed, involving both proton and hydride transfers
-
D-Glucose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
in hydride shift mechanism of catalysis Fe2+ is responsible for proton transfer between O1 and O2, and the hydride shift between C1 and C2 is favored by a markedly hydrophobic environment in the active site. The absence of any obvious enzymatic machinery for catalyzing ring opening of the sugar substrates suggests that the pyrococcal enzyme has a preference for straight chain substrates
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
1,3-propanediol biosynthesis (engineered)
-
Amino sugar and nucleotide sugar metabolism
-
Bifidobacterium shunt
-
Biosynthesis of secondary metabolites
-
chitin biosynthesis
-
formaldehyde oxidation I
-
GDP-mannose biosynthesis
-
gluconeogenesis I
-
gluconeogenesis II (Methanobacterium thermoautotrophicum)
-
gluconeogenesis III
-
Glycolysis / Gluconeogenesis
-
glycolysis I (from glucose-6P)
-
glycolysis III (from glucose)
-
glycolysis V (Pyrococcus)
-
glycolysis VI (metazoan)
-
heterolactic fermentation
-
homolactic fermentation
-
mannitol cycle
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Pentose phosphate pathway
-
sorbitol biosynthesis I
-
Starch and sucrose metabolism
-
starch biosynthesis
-
sucrose biosynthesis I (from photosynthesis)
-
sucrose biosynthesis II
-
sucrose biosynthesis III
-
sucrose degradation II (sucrose synthase)
-
sucrose degradation III (sucrose invertase)
-
sucrose degradation IV (sucrose phosphorylase)
-
UDP-N-acetyl-D-galactosamine biosynthesis II
-
UDP-N-acetyl-D-glucosamine biosynthesis I
-
SYSTEMATIC NAME
IUBMB Comments
D-glucose-6-phosphate aldose-ketose-isomerase
Also catalyses the anomerization of D-glucose 6-phosphate.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6-Phosphoglucose isomerase
-
-
-
-
AfcPGI
O28778
-
autocrine motility factor
-
-
autocrine motility factor
-
-
autocrine motility factor
-
-
D-Glucose-6-phosphate isomerase
-
-
-
-
D-glucose-6-phosphate ketol-isomerase
-
-
-
-
G6-PI
C8TDU8
-
Glucose 6-phosphate isomerase
-
-
-
-
Glucose 6-phosphate isomerase
-
-
Glucose phosphate isomerase
-
-
-
-
Glucose phosphoisomerase
-
-
-
-
glucose-6-phosphate isomerase
-
-
glucose-6-phosphate isomerase
Archaeoglobus fulgidus 7324
-
-
-
glucose-6-phosphate isomerase, cytosolic
P34795
-
Glucosephosphate isomerase 2
-
-
-
-
GPI
-
-
-
-
GPI
Dunaliella salina UTEX-LB-1644
B6E5W6
;
-
GPI
P06744
-
Hexose 6-phosphate isomerase
-
-
-
-
Hexose isomerase
-
-
-
-
Hexose monophosphate isomerase
-
-
-
-
Hexose phosphate isomerase
-
-
-
-
Hexosephosphate isomerase
-
-
-
-
Isomerase, glucose phosphate
-
-
-
-
Neuroleukin
-
-
-
-
Neuroleukin
-
-
NLK
-
-
-
-
Oxoisomerase
-
-
-
-
PGI
-
-
-
-
PGI/AMF
-
-
PGI2
-
-
-
-
PGI3
-
-
-
-
PHI
-
-
-
-
Phosphoglucoisomerase
-
-
-
-
Phosphoglucose isomerase
-
-
-
-
Phosphoglucose isomerase
-
-
Phosphoglucose isomerase
O28778
-
Phosphoglucose isomerase
Archaeoglobus fulgidus 7324
-
-
-
Phosphoglucose isomerase
-
-
Phosphoglucose isomerase
-
-
Phosphoglucose isomerase
-
-
Phosphoglucose isomerase
-
-
Phosphoglucose isomerase
-
-
Phosphoglucose isomerase
-
-
Phosphoglucose isomerase
-
-
Phosphoglucose isomerase
-
-
Phosphoglucose isomerase
P64192
-
Phosphoglucose isomerase
-
-
Phosphoglucose isomerase
-
-
Phosphoglucose isomerase
P83194
-
Phosphoglucose isomerase
-
-
Phosphoglucose isomerase
P13377
-
Phosphoglucose isomerase
Trypanosoma brucei Treu 927
P13377
-
-
phosphoglucose isomerase/autocrine motility factor
-
-
Phosphohexoisomerase
-
-
-
-
Phosphohexomutase
-
-
-
-
Phosphohexose isomerase
-
-
-
-
Phosphohexose isomerase
-
-
Phosphosaccharomutase
-
-
-
-
SA-36
-
-
-
-
Sperm antigen-36
-
-
-
-
VEG54
-
-
-
-
Vegetative protein 54
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-41-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
Swissprot
Manually annotated by BRENDA team
Spanish, Indian and American honeybee
-
-
Manually annotated by BRENDA team
syncytia induced by nematode Heterodera schachtii
UniProt
Manually annotated by BRENDA team
Archaeoglobus fulgidus 7324
-
-
-
Manually annotated by BRENDA team
plastid and cytosolic isoenzyme
-
-
Manually annotated by BRENDA team
Cassia coluteoides
isoenzyme PGI I and II
-
-
Manually annotated by BRENDA team
collected from the Mar Menor coastal lagoon
-
-
Manually annotated by BRENDA team
Dunaliella salina UTEX-LB-1644
UTEX-LB-1644
UniProt
Manually annotated by BRENDA team
H, Wey, and Wis strains
UniProt
Manually annotated by BRENDA team
Entamoeba sp.
-
-
-
Manually annotated by BRENDA team
phosphoglucose isomerase-like activity associated with the carboxy-terminal domains of glucosamine-6-phosphate synthase
-
-
Manually annotated by BRENDA team
Escherichia coli K10
K10
-
-
Manually annotated by BRENDA team
plastid and cytosolic isoenzyme
-
-
Manually annotated by BRENDA team
4 isoforms: 1, 2 ,3 and 4
-
-
Manually annotated by BRENDA team
autocrine motility factor/glucose-6-phosphate isomerase
-
-
Manually annotated by BRENDA team
isozymes PGI1-PGI3
-
-
Manually annotated by BRENDA team
native enzyme and mutant enzymes Thr5 to Ile, Thr224 to Met, Gln343 to Arg, and Asp539 to Asn
-
-
Manually annotated by BRENDA team
patient suffering chronic nonspherocytic hemolytic anemia
-
-
Manually annotated by BRENDA team
patients with inflammatory arthritic diseases
-
-
Manually annotated by BRENDA team
patients with rheumatid arthritis
-
-
Manually annotated by BRENDA team
phosphoglucose isomerase/autocrine motility factor
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
bifunctional phosphoglucose isomerase/phosphomannose isomerase, EC 5.3.1.9 and 5.3.1.8, resp.
Uniprot
Manually annotated by BRENDA team
bifunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.8 and EC5.3.1.9, overexpression in Escherichia coli
-
-
Manually annotated by BRENDA team
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
-
-
Manually annotated by BRENDA team
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
Uniprot
Manually annotated by BRENDA team
enzyme additionally acts as an aldehyde isomerase converting malondialdehyde to methylglyoxal
-
-
Manually annotated by BRENDA team
3 isoenzymes
-
-
Manually annotated by BRENDA team
multiple forms
-
-
Manually annotated by BRENDA team
serovar typhimurium
-
-
Manually annotated by BRENDA team
plastid and cytosolic isoenzyme
-
-
Manually annotated by BRENDA team
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8 resp.
Swissprot
Manually annotated by BRENDA team
strain Treu 927 GUTat 10.1
UniProt
Manually annotated by BRENDA team
Trypanosoma brucei Treu 927
strain Treu 927 GUTat 10.1
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
P06744
deficiency of the enzymatic activity in red blood cells causes nonspherocytic hemolytic anemia
malfunction
-
PGI/AMF is correlated with breast cancer and poor prognosis in breast cancer. Inhibition of PGI/AMF expression triggers mesenchymal-to-epithelial transition in aggressive mesenchymal-type breast cancer MD-MB-231 cells
malfunction
-
neuromuscular symptoms are associated with inherited GPI deficiency
metabolism
-
PGI is a key enzyme in glycolysis and glycogenesis catalyzing the second step of glycolysis
metabolism
-
key enzyme in the AMF signaling pathway, overview
metabolism
-
GPI plays an important role in glycolysis
metabolism
-
PGI is the second enzyme of glycolysis
metabolism
P13377
PGI is the second enzyme of glycolysis
metabolism
-
phosphoglucose isomerase is a key enzyme in the glycolysis and glycogenesis pathways
metabolism
Trypanosoma brucei Treu 927
-
PGI is the second enzyme of glycolysis
-
physiological function
-
PGI/AMF is a housekeeping gene product/cytokine that catalyzes a step in glycolysis and gluconeogenesis, and acts as a multifunctional cytokine associated with aggessive tumors. PGI/AMF induces a mesenchymal-like morphologic conversion being a key enzyme for both epithelial-to-mesenchymal transition in the initiating step of cancer metastasis and mesenchymal-to-epithelial transition in the late stage of metastasis during breast cancer progression, overview
physiological function
-
multifunctional protein GPI is an endogenous inhibitor to myofibril-bound serine proteinase, and may play a significant role in the regulation of muscular protein metabolism in vivo
physiological function
-
AMF is critical for the migration, invasion, metastasis, and anti-apoptotic effects of malignant tumor cells, and its multiple roles in tumor progression may be mediated by certain downstream pathways and effectors. Phosphoglucose isomerase/autocrine motility factor promotes melanoma cell migration through ERK activation dependent on autocrine production of interleukin-8, overview
physiological function
-, P64192
phosphoglucose isomerase plays a key role in both glycolysis and gluconeogenesis inside the cell, whereas outside the cell it exhibits cytokine properties. The enzyme also acts as an autocrine motility factor, a neuroleukin agent and a differentiation and maturation mediator
physiological function
-
the Pgi activity is limiting in the control BL310 strain during growth on lactose or galactose. The level of Pgi enzyme activity controls the level of production of those UDP-glucose and UDP-galactose in galactose
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
Archaeoglobus fulgidus 7324
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-, Q9YE01
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
Q9HIC2, -
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
P06744
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-, O28778
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
Archaeoglobus fulgidus 7324
-
-, the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
D-fructose 6-phosphate
D-mannose 6-phosphate
show the reaction diagram
-, Q9YE01
-
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
show the reaction diagram
Q9HIC2, -
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
P83194
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
-
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-, Q9YE01
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
Q9HIC2, -
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
P06744
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
B6E5W6
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
P13377
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-, P64192
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-, Q9N1E2
the active site residues Lys58 and His388 might be involved in catalytic mechanism
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-, Q9N1E2
in the cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
P13377
the glucose 6-phosphate molecule is bound in an extended conformation in the active site of PGI, substrate binding structure, overview
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
in hydride shift mechanism of catalysis Fe2+ is responsible for proton transfer between O1 and O2, and the hydride shift between C1 and C2 is favored by a markedly hydrophobic environment in the active site. The absence of any obvious enzymatic machinery for catalyzing ring opening of the sugar substrates suggests that the pyrococcal enzyme has a preference for straight chain substrates. The metabolism in extreme thermophiles may use sugars in both ring and straight chain forms. At the extreme temperatures in which Pyrococcus furiosus exists, the equilibrium would increasingly favor the open chain forms
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
Trypanosoma brucei Treu 927
P13377
-, the glucose 6-phosphate molecule is bound in an extended conformation in the active site of PGI, substrate binding structure, overview
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
Dunaliella salina UTEX-LB-1644
B6E5W6
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
Dunaliella salina UTEX-LB-1644
-
-
-
-
r
D-glucose 6-phosphate
fructose 6-phosphate
show the reaction diagram
-
multistep catalytic mechanism is proposed: first the enzyme catalyzes ring opening to yield the open chain form of the substrate. Then isomerization proceeds via proton transfer between C2 and C1 of a cis-enediol(ate) intermediate to yield the open chain form of the product. His388 promotes ring opening by protonating the ring oxygen. Glu216 helps to position His388, and a water molecule that is held in position by Lys518 and Thr214 accepts a proton from the hydroxyl group at C2
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-, Q9YE01
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
Q9HIC2, -
-
-
-
r
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
-
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
-
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
-
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
-
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
-
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
-
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
-
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
-
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
Schistosoma mansoni, Entamoeba sp.
-
-
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
r
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
r
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
r
-
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
r
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
r
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
r
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
r
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
r
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
r
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
r
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
r
-
-
-
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
-
r
-
-
fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
P84140, -
-
-
r
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
-
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
-
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
-
-
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
-
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
-
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
-
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
-
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
-
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
r
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
r
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
r
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
r
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
r
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
r
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
r
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
r
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
r
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
r
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
r
-
-
-
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
-
r
-
-
L-talose
L-tagatose
show the reaction diagram
-
best aldose substrate
-
-
?
malonic dialdehyde
methylglyoxal
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
the enzyme has cell-motility-stimulating activity on mouse colon cancer cells
-
?
additional information
?
-
-
glycolytic enzyme
-
-
-
additional information
?
-
-
glycolytic enzyme
-
-
-
additional information
?
-
-
probable role of the enzyme in starch biosynthesis in amyloplasts
-
-
-
additional information
?
-
-
enzyme of the oxidative pentose phosphate cycle
-
-
-
additional information
?
-
-
the formation of phosphoglucose isomerase is under respiratory control, during anaerobiosis the enzyme is derepressed parallely with other glycolytic enzymes
-
-
-
additional information
?
-
-
the enzyme is part of the glycolytic pathway
-
?
additional information
?
-
-
the enzyme plays a central role in both the glycolysis and the gluconeogenesis pathways
-
?
additional information
?
-
-
the enzyme plays important roles in glycolysis and gluconeogenesis
-
?
additional information
?
-
-
PGI/AMF stimulates beta-catenin expression and is involved in E-cadherin and beta-catenin expression regulation, overview
-
-
-
additional information
?
-
P06744
the enzyme can also act as an autocrine motility factor, neuroleukin, and maturation factor
-
-
-
additional information
?
-
-
the multifunctional protein GPI shows specific and competitive inhibitory activity toward a myofibril-bound serine proteinase, MBSP, from Carassius auratus with a Ki of 320 nM, inhibition kinetics, while no inhibitory activity is identified toward other serine proteinases, such as white croaker MBSP and crucian carp trypsin, overview
-
-
-
additional information
?
-
-
glucose-6-phosphate isomerase catalyzes the interconversion between two different aldoses and ketose for pentoses and hexoses via two isomerization reactions. Activity order as follows: aldose substrates with hydroxyl groups oriented in the same direction at C2, C3, and C4 better than C2 and C4 better than C2 and C3 better than C3 and C4. L-Talose and D-ribulose exhibit the most preferred substrates among the aldoses and ketoses, respectively, substrate specificity, overview
-
-
-
additional information
?
-
Escherichia coli K10
-
the formation of phosphoglucose isomerase is under respiratory control, during anaerobiosis the enzyme is derepressed parallely with other glycolytic enzymes
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
P06744
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
Archaeoglobus fulgidus, Archaeoglobus fulgidus 7324
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
P06744
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
B6E5W6
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
P13377
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-, Q9N1E2
in the cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
Trypanosoma brucei Treu 927
P13377
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
Dunaliella salina UTEX-LB-1644
B6E5W6
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
Dunaliella salina UTEX-LB-1644
-
-
-
-
r
additional information
?
-
-
glycolytic enzyme
-
-
-
additional information
?
-
-
glycolytic enzyme
-
-
-
additional information
?
-
-
probable role of the enzyme in starch biosynthesis in amyloplasts
-
-
-
additional information
?
-
-
enzyme of the oxidative pentose phosphate cycle
-
-
-
additional information
?
-
-
the formation of phosphoglucose isomerase is under respiratory control, during anaerobiosis the enzyme is derepressed parallely with other glycolytic enzymes
-
-
-
additional information
?
-
-
the enzyme is part of the glycolytic pathway
-
?
additional information
?
-
-
the enzyme plays a central role in both the glycolysis and the gluconeogenesis pathways
-
?
additional information
?
-
-
the enzyme plays important roles in glycolysis and gluconeogenesis
-
?
additional information
?
-
-
PGI/AMF stimulates beta-catenin expression and is involved in E-cadherin and beta-catenin expression regulation, overview
-
-
-
additional information
?
-
P06744
the enzyme can also act as an autocrine motility factor, neuroleukin, and maturation factor
-
-
-
additional information
?
-
-
the multifunctional protein GPI shows specific and competitive inhibitory activity toward a myofibril-bound serine proteinase, MBSP, from Carassius auratus with a Ki of 320 nM, inhibition kinetics, while no inhibitory activity is identified toward other serine proteinases, such as white croaker MBSP and crucian carp trypsin, overview
-
-
-
additional information
?
-
Escherichia coli K10
-
the formation of phosphoglucose isomerase is under respiratory control, during anaerobiosis the enzyme is derepressed parallely with other glycolytic enzymes
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
activates 5.2fold 1.5 mM
Cu2+
-
activates 1.3fold 1.5 mM
Fe2+
P84140, -
10 mM, 37C, 156% enhancement of the activity of the wild-type enzyme, mutant enzymes H89A, H91A, E98V and H137A do not contain iron or zinc
Fe2+
-
bound to the enzyme. Catalytic activity is not strongly influenced either by the replacement of Fe2+ by a range of transition metals or by the presence or absence of the bound metal ion. The metal may not directly involved in catalysis but rather may be implicated in substrate recognition
Fe2+
-
activates 3.9fold 1.5 mM
Iron
P84140, -
wild-type enzyme contains 1.25 mol iron per mol of dimer, mutant enzymes H89A, H91A, E98V and H137A do not contain iron or zinc
Mg2+
-
activates 4.7fold 1.5 mM
Mg2+
-
activates
Ni2+
-
activates 4.5fold 1.5 mM
Zinc
P84140, -
wild-type enzyme contains 0.24 mol zinc per mol of dimer
Zn2+
-
activates 4.2fold 1.5 mM
Mn2+
-
activates 1.7fold 1.5 mM
additional information
-
no requirement for Na+, K+, Mg2+, Ca2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,5-Anhydroglucitol 6-phosphate
-
-
2-amino-2-deoxy-D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-amino-2-deoxy-D-glucitol 6-phosphate dimethyl ester
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-amino-2-deoxy-D-mannitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-Deoxy-D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-deoxyglucose 6-phosphate
-
-
3-phosphoglycerate
-
-
5-phospho-D-arabinoamide
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
5-phospho-D-arabinoate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
5-phospho-D-arabinohydroxamate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
5-phospho-D-arabinonate
-
-
5-phospho-D-arabinonate
-
-
5-phospho-D-arabinonate
-
competitive
5-phospho-D-arabinonohydroxamate
-
competitive, stable analogue of putative cis-endiol intermediate
-
5-phosphoarabinonate
-, Q8ZWV0
-
5-phosphoarabinonhydroxamic acid
-
-
5-phosphoarabinonhydroxamic acid
P13377
competitive inhibition
6-phospho-2-deoxygluconate
Cassia coluteoides
-
glucose 6-phosphate as substrate
6-phospho-D-gluconate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
6-phospho-D-gluconoamide
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
6-phosphogluconate
Entamoeba sp.
-
-
6-phosphogluconate
Cassia coluteoides
-
glucose 6-phosphate as substrate
6-phosphogluconate
-
-
6-phosphogluconate
-
-
6-phosphogluconate
-
-
6-phosphogluconate
-
0.2 mM, 52% inhibition
6-phosphogluconate
-
-
6-phosphogluconate
-
competitive
6-phosphogluconate
-
-
6-phosphogluconate
-
-
6-phosphogluconate
-
-
6-phosphogluconate
-
competitive
6-phosphogluconate
-
-
6-phosphogluconate
-, Q9YE01
-
6-phosphogluconate
Q9HIC2, -
-
6-phosphogluconate
-
pH 7.6, 25C
6-Phosphomannonate
Cassia coluteoides
-
with glucose 6-phosphate as substrate
Agaricic acid
-
-
Agaricic acid
P13377
irreversible inhibition
Ca2+
-
slight inhibition at 1.5 mM
Cd2+
P84140, -
10 mM, 96% inhibition, D-fructose 6-phosphate as substrate
Co2+
P84140, -
10 mM, 59% inhibition, D-fructose 6-phosphate as substrate
Cu2+
P84140, -
10 mM, 96% inhibition, D-fructose 6-phosphate as substrate
D-fructose 1,6-bisphosphate
P84140, -
-
D-fructose 1,6-bisphosphate
-
-
D-Fructose 1-phosphate
P84140, -
-
D-Fructose 1-phosphate
-
-
D-Glucal 6-phosphate
-
-
D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
D-gluconate 6-phosphate
-
-
D-gluconate 6-phosphate
P84140, -
-
D-mannose 6-phosphate
P84140, -
-
D-mannose 6-phosphate
-
-
dihydroxyacetone phosphate
-
-
EDTA
P84140, -
10 mM, 78% inhibition, D-fructose 6-phosphate as substrate
EDTA
-
complete inhibition
EDTA
-
100fold excess, complete loss of activity within 10 min. 93% of activity may be recovered by additon of 1000fold excess of Zn2+
EDTA
-
strong inhibition
Erythritol 4-phosphate
-
-
erythrose 4-phosphate
-
-
erythrose 4-phosphate
Cassia coluteoides
-
glucose 6-phosphate as substrate
erythrose 4-phosphate
-
activates enzyme form B with ribose 5-phosphate as substrate, inhibits activity of enzyme form A and B with glucose 6-phosphate as substrate, inhibits activity of enzyme form A with glucose 6-phosphate as substrate
erythrose 4-phosphate
-
0.02 mM, 58% inhibition
erythrose 4-phosphate
-
competitive
erythrose 4-phosphate
-
competitive
erythrose 4-phosphate
-, Q9YE01
-
erythrose 4-phosphate
Q9HIC2, -
-
erythrose-4-phosphate
-
-
fructose 1,6-diphosphate
-
-
fructose 1,6-diphosphate
-
1 mM, 4% inhibition
fructose 1-phosphate
-
-
fructose 1-phosphate
-
1 mM, 10% inhibition
gluconate 6-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
insulin-like growth factor binding protein-3
-
both glycosylated and unglycosylated, binding and inhibition of enzyme
-
K+
P84140, -
10 mM, 18% inhibition, D-fructose 6-phosphate as substrate
L-Sorbose 6-phosphate
-
-
L-Xylulose 5-phosphate
-
-
Maleate
-
10 mM, 50% inhibition
-
Maleic anhydride
-
-
malonate
-
10 mM, 15% inhibition
mannitol 1-phosphate
Cassia coluteoides
-
glucose 6-phosphate as substrate
mannitol 6-phosphate
-
-
mannose 6-phosphate
-
-
N-acetyl-2-amino-2-deoxy-D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
N-bromoacetylethanolamine phosphate
-
-
Ni2+
P84140, -
10 mM, 84% inhibition, D-fructose 6-phosphate as substrate
oxaloacetate
-
10 mM, 25% inhibition
oxoglutarate
-
10 mM, 20% inhibition
ribose 5-phosphate
-
-
ribose 5-phosphate
-
1 mM, 12% inhibition
ribose 5-phosphate
-
-
ribulose 5-phosphate
-
-
ribulose 5-phosphate
-
0.5 mM, 48% inhibition
ribulose 5-phosphate
-
-
sedoheptulose 7-phosphate
-
-
sedoheptulose 7-phosphate
-
1 mM, 10% inhibition
sorbitol 6-phosphate
-
-
suramin
-
no inhibition
suramin
P13377
an anti-trypanosomal drug
Zn2+
-
plastid enzyme is completely inhibited by 5 mM, activity of cytosolic isoenzyme is reduced to 49% of untreated control
Zn2+
P84140, -
10 mM, 89% inhibition, D-fructose 6-phosphate as substrate
Mn2+
P84140, -
10 mM, 18% inhibition, D-fructose 6-phosphate as substrate
additional information
-
no inhibition by PCMB and iodoacetate
-
additional information
-
not inhibitory: EDTA
-
additional information
-
screening for thiazolide inhibitors, diverse compounds, mode of action of thiazolides and structure-activity relationship, overview
-
additional information
-
no inhibition by suramin, an anti-trypanosomal drug, and agaricic acid
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Zn2+
-
the coordination shell of Zn2+ changes significantly from the initial static crystal conformation to the equilibrated state of the enzyme-D-fructose 6-phosphate complex. Although Zn2+ is not directly involved in the reaction, the metal ion as a structural anchor constructs a hydrogen bond wire to connect the substrate to the outer region, providing a potential channel for hydrogen exchange between the substrate and solvent
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.031
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant S278L
0.034
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant I525T
0.037
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant wild-type enzyme
0.038
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant R347H; pH 7.5, 30C, recombinant mutant R75G
0.039
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant L487F
0.04
-
D-fructose 6-phosphate
-
50C, pH 6.3
0.045
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant A300P; pH 7.5, 30C, recombinant mutant L339P
0.046
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant R347C; pH 7.5, 30C, recombinant mutant T375R
0.05
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant E495K
0.06
-
D-fructose 6-phosphate
-
pH 7.4, 80C
0.061
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant R83W
0.063
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant T195I; pH 7.5, 30C, recombinant mutant V101M
0.068
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant R472H
0.147
-
D-fructose 6-phosphate
-
22C, pH 7.4
0.18
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme Y95K
0.19
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme H136A
0.2
-
D-fructose 6-phosphate
Q9HIC2, -
80C, pH 7.4
0.21
-
D-fructose 6-phosphate
-, Q9YE01
50C, pH 7.4
0.22
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme T63A
0.25
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, wild-type enzyme
0.27
-
D-fructose 6-phosphate
-
pH 7.6, 25C
0.3
-
D-fructose 6-phosphate
-
pH 7.4, 50C
0.318
-
D-fructose 6-phosphate
-
pH 7.6, 22C
0.36
-
D-fructose 6-phosphate
-
pH 8.0
0.36
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme Y95F
0.39
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme H80D
0.42
-
D-fructose 6-phosphate
-
50C, pH 7.0, recombinant enzyme
0.44
-
D-fructose 6-phosphate
-, Q9YE01
80C, pH 7.4
0.5
-
D-fructose 6-phosphate
-
50C
0.5
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme G79A
0.59
-
D-fructose 6-phosphate
P84140, -
50C, pH 7.5, mutant enzyme E89V
0.6
-
D-fructose 6-phosphate
-
pH 7.4, 50C
0.63
-
D-fructose 6-phosphate
-
50C, pH 7.0, native enzyme
0.7
-
D-fructose 6-phosphate
-
pH 7.6, 37C
0.8
-
D-fructose 6-phosphate
-
pH 7.4, 50C
1
-
D-fructose 6-phosphate
-
80C, pH 7.0, native enzyme
1.2
-
D-fructose 6-phosphate
-
80C, pH 7.0, recombinant enzyme
1.4
-
D-fructose 6-phosphate
P84140, -
50C, pH 7.5, mutant enzyme H137A
1.4
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme Y160F
1.7
-
D-fructose 6-phosphate
P84140, -
50C, pH 7.5, wild-type enzyme
2
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme G79L; pH 7.4, 70C, mutant enzyme H82A
2.1
-
D-fructose 6-phosphate
P84140, -
50C, pH 7.5, mutant enzyme H91A
2.9
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme E93D
3
-
D-fructose 6-phosphate
-
pH 7.2, 37C
3.5
-
D-fructose 6-phosphate
P84140, -
50C, pH 7.5, mutant enzyme H89A
4
-
D-fructose 6-phosphate
-
80C, pH not specified in the publication
20.3
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme H80A
169
-
D-fructose 6-phosphate
-
wild-type, 37C, pH 8.0
170
-
D-fructose 6-phosphate
-
mutant A346H, 37C, pH 8.0
0.11
-
D-glucose 6-phosphate
-
ZR-82 cells, 22C
0.28
-
D-glucose 6-phosphate
-
22C, pH 7.4
0.4
-
D-glucose 6-phosphate
-
pH 7.4, 50C
0.6
-
D-glucose 6-phosphate
-
pH 7.4, 50C
0.72
-
D-glucose 6-phosphate
Q9HIC2, -
80C, pH 7.4
1
-
D-glucose 6-phosphate
-
50C, pH 6.3
1
-
D-glucose 6-phosphate
-
pH 7.6, 37C
1
-
D-glucose 6-phosphate
-
pH 7.2, 37C
1.02
-
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37C
1.53
-
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37C
1.65
-
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60C
1.86
-
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60C
1.9
-
D-glucose 6-phosphate
-
pH 7.4, 80C
1.9
-
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37C
1.99
-
D-glucose 6-phosphate
-
50C, pH 7.0, native enzyme
2
-
D-glucose 6-phosphate
-
50C, pH 7.0, recombinant enzyme
2.11
-
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37C
2.43
-
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60C
2.58
-
D-glucose 6-phosphate
-
mutant GroD1 cells, 22C
2.7
-
D-glucose 6-phosphate
-
pH 7.4, 50C
2.89
-
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60C
3.5
-
D-glucose 6-phosphate
-, Q9YE01
80C, pH 7.4
7.9
-
D-glucose 6-phosphate
-
80C, pH 7.0, recombinant enzyme
8.7
-
D-glucose 6-phosphate
-
80C, pH 7.0, native enzyme
11.7
-
D-glucose 6-phosphate
P84140, -
50C, pH 7.5, wild-type enzyme
221
-
D-glucose 6-phosphate
-
wild-type, 37C, pH 8.0
267.4
-
D-glucose 6-phosphate
-
mutant A346H, 37C, pH 8.0
0.25
-
D-mannose 6-phosphate
Q9HIC2, -
80C, pH 7.4
1.1
-
D-mannose 6-phosphate
-, Q9YE01
80C, pH 7.4
0.01
0.17
fructose 6-phosphate
-
muscle enzyme, values of 0.01 mM, 0.12 mM and 0.17 mM are determined by different authors
0.0186
-
fructose 6-phosphate
-
isomerase a
0.0205
-
fructose 6-phosphate
-
isomerase c
0.0213
-
fructose 6-phosphate
-
isomerase b
0.048
-
fructose 6-phosphate
-
-
0.0596
-
fructose 6-phosphate
-
mutant enzyme Thr224 to Met
0.0635
-
fructose 6-phosphate
-
native enzyme
0.0657
-
fructose 6-phosphate
-
mutant enzyme Thr5 to Ile
0.07
-
fructose 6-phosphate
-
mammary gland enzyme
0.071
-
fructose 6-phosphate
-
-
0.0734
-
fructose 6-phosphate
-
mutant enzyme Asp539 to Asn
0.0769
-
fructose 6-phosphate
-
mutant enzyme Gln343 to Arg
0.09
-
fructose 6-phosphate
-
isozyme 1 and isozyme 2
0.1
-
fructose 6-phosphate
-
-
0.1
-
fructose 6-phosphate
-
glucose 6-phosphate, soluble enzyme
0.1
-
fructose 6-phosphate
-
fructose 6-phosphate, isozyme 4
0.11
0.23
fructose 6-phosphate
-
values of 0.11 mM, 0.15 mM and 0.23 mM are determined by different autors
0.11
-
fructose 6-phosphate
-
isozyme 3
0.116
-
fructose 6-phosphate
-
-
0.119
-
fructose 6-phosphate
-
-
0.12
-
fructose 6-phosphate
-
-
0.12
-
fructose 6-phosphate
-
liver enzyme
0.12
-
fructose 6-phosphate
-
glucose 6-phosphate
0.12
-
fructose 6-phosphate
-
fructose 6-phosphate, at pH 8.6
0.12
-
fructose 6-phosphate
-
fructose 6-phosphate, enzyme form PGI II
0.122
-
fructose 6-phosphate
-
-
0.14
-
fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from germinating seeds
0.1425
-
fructose 6-phosphate
-
-
0.167
-
fructose 6-phosphate
-
-
0.17
-
fructose 6-phosphate
-
enzyme form PGI I
0.18
-
fructose 6-phosphate
-
-
0.2
-
fructose 6-phosphate
-
enzyme forms PGI I and PGI II
0.2
-
fructose 6-phosphate
-
glucose 6-phosphate, immobilized enzyme
0.21
-
fructose 6-phosphate
-
erythrocyte enzyme, wild-type
0.228
0.278
fructose 6-phosphate
-
-
0.23
-
fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from developing seeds
0.3
-
fructose 6-phosphate
-
isozyme 1 and 2
0.35
-
fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from germinating seeds
0.46
-
fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from developing seeds
0.46
-
fructose 6-phosphate
-
glucose 6-phosphate, isozyme 2
0.48
-
fructose 6-phosphate
-
chloroplastic isoenzyme
0.74
-
fructose 6-phosphate
-
erythrocyte enzyme, mutant B9
0.03
0.8
glucose 6-phosphate
-
muscle enzyme, values of 0.03 mM, 0.31 mM and 0.8 mM are determined by different authors
0.12
0.57
glucose 6-phosphate
-
mammary gland enzyme, values of 0.12 mM and 0.57 mM are determined by different authors
0.25
-
glucose 6-phosphate
-
-
0.27
-
glucose 6-phosphate
-
-
0.3
1.5
glucose 6-phosphate
-
values of 0.27 mM, 0.3 mM, 0.7 mM, 0.8 mM and 1.5 mM are determined by different authors
0.351
-
glucose 6-phosphate
-
mutant enzyme Thr224 to Met
0.36
-
glucose 6-phosphate
-
-
0.44
-
glucose 6-phosphate
-
at pH 8.6
0.44
-
glucose 6-phosphate
-
glucose 6-phosphate, enzyme form PGI I and PGI II
0.44
-
glucose 6-phosphate
-
glucose 6-phosphate
0.445
-
glucose 6-phosphate
-
native enzyme
0.449
-
glucose 6-phosphate
-
mutant enzyme Thr5 to Ile
0.45
-
glucose 6-phosphate
-
isozyme 4
0.505
-
glucose 6-phosphate
-
mutant enzyme Asp539 to Asn
0.51
-
glucose 6-phosphate
-
isozyme 1
0.573
-
glucose 6-phosphate
-
mutant enzyme Gln343 to Arg
0.58
-
glucose 6-phosphate
-
isozyme 3
0.58
-
glucose 6-phosphate
-
fructose 6-phosphate, cytosolic isoenzame
0.6
-
glucose 6-phosphate
-
liver enzyme
0.83
-
glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from germinating seeds
1.1
-
glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from germinating seeds
1.3
-
glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from developing seeds
1.5
-
glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from developing seeds
2
-
glucose 6-phosphate
-
-
2
-
glucose 6-phosphate
-
-
5.9
-
glucose 6-phosphate
-
isozyme 2
8
-
glucose 6-phosphate
-
isozyme 1
8
-
glucose 6-phosphate
-
glucose 6-phosphate, cytosolic and chloroplastic isoenzyme
133
-
L-talose
-
pH 7.0, 95C
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
the pH-value has a great influence on the Km-value for fructose 6-phosphate
-
additional information
-
additional information
-
kinetics for aldose substrates, overview
-
additional information
-
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0003
-
D-fructose 6-phosphate
P84140, -
50C, pH 7.5, mutant enzyme E98V
0.021
-
D-fructose 6-phosphate
P84140, -
50C, pH 7.5, mutant enzyme H89A
0.06
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme E93D
0.07
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme G79L
0.22
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme Y95F
0.32
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme G79A
0.34
-
D-fructose 6-phosphate
P84140, -
50C, pH 7.5, mutant enzyme H137A
0.42
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme H80D
0.43
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme H80A
0.5
-
D-fructose 6-phosphate
P84140, -
50C, pH 7.5, mutant enzyme H91A
0.6
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant S278L
0.68
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme Y95K
1.9
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme T63A
8
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme H82A
8.4
-
D-fructose 6-phosphate
-
50C
11.6
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme Y160F
15
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant L339P
18
-
D-fructose 6-phosphate
-
pH 8.0
19
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant L487F
26
-
D-fructose 6-phosphate
P84140, -
50C, pH 7.5, wild-type enzyme
30.8
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme H136A
32.4
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, wild-type enzyme
42
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant R347H
75
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant T375R
76
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant I525T
93
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant R75G
100
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant A300P
150
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant R347C
160
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant V101M
190
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant R472H; pH 7.5, 30C, recombinant mutant R83W
300
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant T195I
420
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant E495K
650
-
D-fructose 6-phosphate
P06744
pH 7.5, 30C, recombinant wild-type enzyme
0.3
-
D-glucose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant S278L
17
-
D-glucose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant L487F
31
-
D-glucose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant L339P
42
-
D-glucose 6-phosphate
P84140, -
50C, pH 7.5, wild-type enzyme
61
-
D-glucose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant A300P
63
-
D-glucose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant R347H
80
-
D-glucose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant T375R
110
-
D-glucose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant I525T
120
-
D-glucose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant R83W
130
-
D-glucose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant R75G
140
-
D-glucose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant V101M
260
-
D-glucose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant R472H
350
-
D-glucose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant R347C
380
-
D-glucose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant T195I
729
-
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37C
750
-
D-glucose 6-phosphate
P06744
pH 7.5, 30C, recombinant mutant E495K
929
-
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37C
946
-
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37C
1000
-
D-glucose 6-phosphate
P06744
pH 7.5, 30C, recombinant wild-type enzyme
1091
-
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37C
2009
-
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60C
2198
-
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60C
2433
-
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60C
2765
-
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60C
3330
-
fructose 6-phosphate
-
isomerase a
475.5
-
L-talose
-
pH 7.0, 95C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.02
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme E93D; pH 7.4, 70C, mutant enzyme H80A
9143
0.035
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme G79L
9143
0.61
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme Y95F
9143
0.64
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme G79A
9143
1.1
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme H80D
9143
3.8
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme Y95K
9143
4
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme H82A
9143
8.3
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme Y160F
9143
8.6
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme T63A
9143
130
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, wild-type enzyme
9143
162
-
D-fructose 6-phosphate
-, O28778
pH 7.4, 70C, mutant enzyme H136A
9143
489
-
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37C
9206
517
-
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37C
9206
618
-
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37C
9206
715
-
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37C
9206
906
-
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60C
9206
957
-
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60C
9206
1218
-
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60C
9206
1308
-
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60C
9206
3.58
-
L-talose
-
pH 7.0, 95C
224738
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
12.3
-
2-amino-2-deoxy-D-glucitol 6-phosphate
-
pH 8.0
17.2
-
2-amino-2-deoxy-D-mannitol 6-phosphate
-
pH 8.0
0.68
-
2-Deoxy-D-glucitol 6-phosphate
-
pH 8.0
0.0046
-
5-phospho-D-arabinoamide
-
pH 8.0
0.0022
-
5-phospho-D-arabinoate
-
pH 8.0
0.27
-
5-phospho-D-arabinonate
-
50C
0.005
-
5-phospho-D-arabinonohydroxamate
-
50C
-
0.148
-
6-phospho-D-gluconate
-
pH 8.0
0.56
-
6-phospho-D-gluconoamide
-
pH 8.0
0.02
-
6-phosphogluconate
-
50C, pH 6.3
0.11
-
6-phosphogluconate
-
pH 7.4, 50C
0.15
-
6-phosphogluconate
-
pH 7.6, 37C
0.67
-
6-phosphogluconate
-
pH 7.4, 50C
2
10
6-phosphogluconate
Q9HIC2, -
80C, pH 7.4
3
-
6-phosphogluconate
-
pH 7.2, 37C
58
-
6-phosphogluconate
-, Q9YE01
80C, pH 7.4
12
-
D-fructose 1,6-bisphosphate
P84140, -
50C, pH 7.5, D-fructose 6-phosphate as substrate
4
-
D-Fructose 1-phosphate
P84140, -
50C, pH 7.5, D-fructose 6-phosphate as substrate
0.04
-
D-glucitol 6-phosphate
-
pH 8.0
0.38
-
D-gluconate 6-phosphate
P84140, -
50C, pH 7.5, D-fructose 6-phosphate as substrate
2.3
-
D-mannose 6-phosphate
P84140, -
50C, pH 7.5, D-fructose 6-phosphate as substrate
2
10
EDTA
-
pH 7.4, 50C
97
-
EDTA
-
pH 7.4, 50C
101
-
EDTA
-
pH 7.6, 37C
120
-
EDTA
-
pH 7.2, 37C
0.035
-
erythrose 4-phosphate
-, Q9YE01
80C, pH 7.4
0.06
-
erythrose 4-phosphate
-
50C, pH 6.3
0.164
-
erythrose 4-phosphate
Q9HIC2, -
80C, pH 7.4
1.8
-
erythrose 4-phosphate
-
pH 7.4, 50C
0.0014
-
erythrose-4-phosphate
-
pH 7.4, 50C
0.8
-
gluconate 6-phosphate
-
pH 7.6, 22C
10
-
Maleate
-
-
-
0.076
-
N-acetyl-2-amino-2-deoxy-D-glucitol 6-phosphate
-
pH 8.0
0.03
-
sorbitol-6-phosphate
-
pH 7.6, 37C
0.36
-
sorbitol-6-phosphate
-
pH 7.2, 37C
0.54
-
sorbitol-6-phosphate
-
pH 7.4, 50C
0.7
-
sorbitol-6-phosphate
-
pH 7.4, 50C
0.29
-
suramin
P13377
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00005
-
5-phosphoarabinonhydroxamic acid
P13377
-
0.0002
-
5-phosphoarabinonhydroxamic acid
-
-
0.01
-
Agaricic acid
P13377
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.06
-
-
substrate: D-fructose 6-phosphate, 80C, pH not specified in the publication
0.39
-
-
purified native enzyme
7.7
-
-
50C, pH 7.0
12
-
-
70C, pH 7.0
14.5
-
-
50C, pH 7.0, reaction with D-fructose 6-phosphate
29.1
-
-
50C, pH 7.0, reaction with D-glucose 6-phosphate
47.3
-
P84140, -
formation of D-glucose 6-phosphate
48.5
-
P13377
purified recombinant His-tagged enzyme
140
-
-
purified enzyme, substrate fructose 6-phosphate, reverse reaction
212.6
-
-
22C, pH 7.4
500
-
-
D-glucose 6-phosphate formation, isomerase c
520
-
-
-
600
-
-
D-glucose 6-phosphate formation, isomerase b
617.7
-
-
pH 7.6, 22C
620
-
-
with substrate L-talose
620
-
P06744
purified wild-type enzyme
870
-
-
D-glucose 6-phosphate formation, isomerase a
1470
-
-
fructose 6-phosphate formation
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
mass spectrometry based method for the direct determination of kinetic konstants of enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
-
-
ribose 5-phosphate, enzyme form A
6
11
Cassia coluteoides
-
isoenzyme PGI I
7
11
Cassia coluteoides
-
isoenzyme PGI II
7
-
-
ribose 5-phosphate, enzyme form B
7
-
-
both directions
7.4
-
-, O28778
assay at
7.5
-
-
glucose 6-phosphate, enzyme forms A and B
7.5
-
P06744
assay at
7.6
-
-, Q9YE01
-
7.6
-
Q9HIC2, -
-
8
-
-
soluble and immobilized enzyme
8
-
-
assay at, reverse reaction
8
-
-
free and immobilized enzyme, in HEPES and TAPS buffers
8.1
-
-
enzyme PGI I
8.1
-
-
Tris-maleate buffer
8.3
-
-
-
8.5
-
-
in Tris-HCl buffer
8.5
-
-
in Tris-HCl buffer
8.6
-
-
enzyme form PGI II
9.5
-
-
in glycine-NaCl-NaOH buffer
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.3
7
-
50% of maximal activity at pH 6.3 and pH 7.0
6
10
-
pH 6.0: about 70% of maximal activity of soluble enzyme, about 30% of maximal activity of immobilized enzyme
6
8
-
about 50% of maximal activity above pH 6.0 and below pH 8.0
6.3
8.8
-
more than 50% of maximum activity in this range
6.5
8.5
-
pH profile, overview
7
10
-
about 50% of maximal activity at pH 7 and at pH 10
7
9
-
free and immobilized enzymes have approximately 75% and 40% of their maximum activity at pH 7.0 and pH 9.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at room temperature
30
-
P06744
assay at
50
55
-
soluble enzyme
50
-
-
immobilized enzyme
60
-
-
free and immobilized enzyme, at pH 7.5
70
-
-, O28778
assay at
80
-
-
assay at
98
-
-, Q9YE01
or above
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
60
-
30C: about 45% of maximal activity of immobilized enzyme, about 35% of maximal activity of soluble enzyme, 60C: about 60% of maximal activity of immobilized enzyme, about 65% of maximal activity of immobilized enzyme
40
98
-
temperature profile, overview
50
70
-
free and immobilized enzymes retain about 90% of their maximum activity at 50C and 70C, but only about 40% of optimum activity is exhibited at 30C
60
95
-
60C: about 30% of maximal activity, 95C: about 30% of maximal activity
70
110
-
70C: about 40% of maximal activity, 110C: about 35% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.22
-
-
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
colon carcinomas show increased PGI expression compared to control cells, overview
Manually annotated by BRENDA team
Archaeoglobus fulgidus 7324
-
-
-
Manually annotated by BRENDA team
Archaeoglobus fulgidus 7324
-
-
-
Manually annotated by BRENDA team
-
3 enzyme variants are due to a specific intracellular cleavage of the enzyme in the malignant cells
Manually annotated by BRENDA team
-
enzyme localizes to actively growing hyphal tips
Manually annotated by BRENDA team
-
plastid and cytosolic isoenzyme
Manually annotated by BRENDA team
-
PGI activity in vesicle fluid
Manually annotated by BRENDA team
-
peripheral blood mononuclear cell
Manually annotated by BRENDA team
Cassia coluteoides
-
developing and germinating
Manually annotated by BRENDA team
-
peroxisome/plasmalogen-deficient variant of the CHO-K1 cell line
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Escherichia coli (strain K12)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Plasmodium falciparum (isolate 3D7)
Plasmodium falciparum (isolate 3D7)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Staphylococcus aureus (strain COL)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
27000
-
-
analytical ultracentrifugation
41000
-
-
native enzyme, gel filtration
43000
-
-
gel filtration
45000
-
-, Q9YE01
gel filtration
48000
-
-
mammary gland, low speed sedimentation without reaching equilibrium
48000
-
Q9HIC2, -
gel filtration
49600
-
-
gel filtration
65000
-
-
sedimentation equilibrium, analytical ultracentrifugation
67000
-
-
gel filtration
67000
-
Q9HIC2, -
analytical ultracentrifugation
67700
-
-
enzyme form B, gel filtration
80000
-
-
gel filtration
96000
-
-
gel filtration
104000
-
-
gel filtration
105000
-
-
gel filtration
110000
120000
-
-
110000
-
-
gel filtration
110000
-
-
sedimentation equilibrium analysis
110000
-
-
gel filtration
116000
-
-
gel filtration
118000
-
-
isoenzymes 1-4, gel filtration
120000
127000
Cassia coluteoides
-
gel filtration, density gradient centrifugation
120000
130000
-
low-molecular weight form PGI I, gel filtration, sucrose density gradient centrifugation
120000
-
-
isoenzyme 1 and 2, sedimentation velocity centrifugation
120000
-
-
isoenzyme A, B and C, sedimentation equilibrium ultracentrifugation, gel electrophoresis
120000
-
-
gel filtration, sucrose density gradient centrifugation
120000
-
-
native PAGE
120000
-
-
-
120000
-
-
gel filtration
120000
-
-
gel filtration
125000
-
-
isomerase a, sedimentation equilibrium analysis
125000
-
-
cytosolic isoenzyme, gel filtration
125000
-
-
gel filtration
125000
-
-
cytosolic isoenzyme, gel filtration
128000
-
-
gel filtration
130000
140000
-
-
130000
-
-
gel filtration
132000
-
-
sedimentation velocity ultracentrifugation
132000
-
-
high speed equilibrium sedimentation
135000
-
-
enzyme form A, gel filtration
140000
-
-
plastidic isoenzyme, gel filtration
145000
-
-
calculation from sedimentation coefficient and diffusion coefficient
172000
-
-
sedimentation equilibrium analysis
202000
204000
-
gel filtration, electrophoresis of the enzyme cross-linked with dimethyl adipimidate
220000
234000
-
high-molecular weight form PGI II, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 56000, enzyme variant C, SDS-PAGE; x * 57000, enzyme variant B, SDS-PAGE; x * 60000, enzyme variant A, SDS-PAGE
?
-
x * 61310, calculation from nucleotide sequence
?
-
x * 67113, calculation from nucleotide sequence
?
-
x * 66000, SDS-PAGE
?
-
x * 50000, SDS-PAGE
?
-
x * 65000, recombinant enzyme, SDS-PAGE
?
-
x * 21476, sequence calculation, x * 21500, SDS-PAGE
?
-
x * 75000, recombinant His-tagged enzyme, SDS-PAGE, x * 73300, about, sequence calculation
?
-
x * 49000, free enzyme, SDS-PAGE
dimer
-
2 * 60000-70000, SDS-PAGE, SDS velocity centrifugation, maleic anhydride velocity and equilibrium sedimentation, urea velocity sedimentation, propionic acid velocity sedimentation guanidine-HCl velocity and equilibrium sedimentation
dimer
-
2 * 70700, isomerase A, SDS-PAGE
dimer
-
2 * 60000-67000, SDS-PAGE
dimer
-
2 * 61000, SDS-PAGE
dimer
-
2 * 63000, sedimentation velocity ultracentrifugation of enzyme dissociated in 6 M guanidine/HCl
dimer
-
2 * 60000, SDS-PAGE, gel filtration in 6 M guanidine-HCl
dimer
-
2 * 34000, enzyme form B, gel filtration after equilibration with SDS
dimer
-
2 * 59000, low-molecular weight form, SDS-PAGE
dimer
-
2 * 63000-67000, SDS-PAGE, analytical ultracentrifugation in 6 M guanidine/HCl
dimer
-
2 * 61000, SDS-PAGE
dimer
-
2 * 59000, isoenzyme 1-5, SDS-PAGE
dimer
-
1 * 6320, A-type subunit, + 1 * 69800, B-type subunit, isoenzyme 3, SDS-PAGE; 2 * 63200, A-type subunit, isoenzyme 1 and 2, SDS-PAGE; 2 * 69800, B-type subunit, isoenzyme 4, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
-
the enzyme is a dimer with two alpha/beta-sandwich domains in each subunit
dimer
-
2 * 23000, SDS-PAGE
dimer
-
2 * 61450, mass spectrometry, 2 * 61000, SDS-PAGE
dimer
-
2 * 36000, SDS-PAGE, 2 * 33548, calculated
dimer
-
2 * 26834, calculated, 2 * 32000, SDS-PAGE
dimer
-
2 * 34684, calculated, 2 * 27000, SDS-PAGE
dimer
-, Q9YE01
2 * 36000, SDS-PAGE, 2 * 36100, calculated
dimer
Q9HIC2, -
2 * 35000, SDS-PAGE, 2 * 35150, calculated
dimer
P13377
structure and active site conformation, overview
dimer
Escherichia coli K10
-
2 * 59000, low-molecular weight form, SDS-PAGE
-
dimer
Trypanosoma brucei Treu 927
-
structure and active site conformation, overview
-
heterodimer
-
1 * 55000 + 1 * 65000, SDS-PAGE
homodimer
P06744
-
homodimer
-, P64192
x-ray crystallography
monomer
-
1 * 27424, calculated, 1 * 28000, SDS-PAGE
tetramer
-
4 * 34000, enzyme form A, gel filtration after equilibration with SDS
tetramer
-
possible 4 * 59000, high-molecular weight form, SDS-PAGE
tetramer
-
4 * 50600, SDS-PAGE
tetramer
Escherichia coli K10
-
possible 4 * 59000, high-molecular weight form, SDS-PAGE
-
monomer
-
1 * 30209, calculated, 1 * 28000, SDS-PAGE
additional information
-
interaction of enzyme with insulin-like growth factor binding protein-3, both glycosylated and unglycosylated, results in formation of a complex of 80 kDa and in dose-dependent inhibition of enzyme
additional information
-
poly(AFP-ribose)polymerase-14, i.e. PARP-14, is a binding partner of phosphoglucose isomerase/autocrine motility factor. Phosphoglucose isomerase/autocrine motility factor is degraded via the ubiquitin-lysosome system, and PARP-14 inhibits the ubiquitination of the enzyme thus contributing to its stabilization and secretion
additional information
-
predicted 2D and 3D structures of GPI proteins possess potential active motifs including GEPGTNGQHSFYQLIHQG and VQGFIWGINSFDQWGVELGK, and critical active site residues, such as Ser241, Ser296, Thr298, Thr301, Arg358, Glu444, His475 and Lys600
additional information
C8TDU8, -
structure homology modelling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no glycoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion method, crystal strcuture at 2.3 A resolution
-
hanging drop vapor diffusion method, crystal structure of the enzyme complexed with 5-phospho-D-arabinonate and N-bromoacetylethanolamine phosphate at 2.5 A and 2.3 A resolution, respectively. The inhibitors bind to a region within the domains interface and interact with His306 from the other subunit
-
native enzyme and enzyme lacking N-terminal 47 amino acids. Comparison of data with mammalian enzymes
-
native enzyme and in complex with glucose 6-phosphate or erythrose 4-phosphate
P06745
hanging drop vapor diffusion method, using 1.2 M ammonium sulfate pH 8.5 (0.1 M HEPES) and 5% (v/v) glycerol at 10C
-, P64192
resolution of 2.8 A, space group I212121
-
enzyme complexed with the competitive inhibitor D-gluconate 6-phosphate, X-ray crystallography at 2.5 A resolution
-
hanging drop vapor diffusion method, X-ray crystal structure of the enzyme complexed with the cyclic form of its substrate, D-fructose 6-phosphate, at 2.1 A resolution
-
in complex with D-sorbitol 6-phosphate
-
purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, mixing 0.002 ml of both protein solution and reservoir solution, the latter containing 38% v/v PEG 400 and 0.2 M calcium acetate in 0.1 M sodium cacodylate-HCl, pH 6.5, equilibration over 0.5 ml of reservoir solution, 1 week, X-ray diffraction structure determination and analysis at 1.5 A resolution
-
both in complex with fructose 6-phosphate and with glucose 6-phosphate
Q8ZWV0
both native form and in complex with 5-phosphoarabinonate
-, Q8ZWV0
1.9 A resolution, crystals belong to the space group P2(1)
-
hanging-drop method of vapour diffusion using 1.6 M sodium citrate as the precipitant at pH 6.5. Maximum resolution of 1.92 A on a single selenomethionine-incorporated crystal. Crystal belongs to space group C2, with approximate unit-cell parameters a = 84.7, b = 42.4, c = 57.3 A, beta = 120.6 and a monomer in the asymmetric unit
-
in presence of bound zinc, substrate D-fructose 6-phosphate and several competitive inhibitors
-
native form and in comlex with 5-phospho-D-arabinonate, in presence and absence of Mn2+
-
structure is determined by X-ray diffraction to 2 A resolution
-
vapor diffusion using the hanging drop method, crystal structure of the enzyme in native form and in complex with two active site ligands, 5-phosphoarabinonate and gluconate 6-phosphate
-
enzyme complexed with glucose 6-phosphate, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
purified recombinant His-tagged enzyme complexed with glucose 6-phosphate, by hanging drop vapor diffusion method at room temperature, 0.004 ml of protein solution with 28.4 mg/ml protein and 5 mM fructose 6-phosphate is mixed with 0.002 ml of reservoir solution containing 10% PEG 3350, 50 mM sodium citrate, and 50 mM dithiothreitol, a few days, X-ray diffraction structure determination and analysis at 1.6 A resolution. Although fructose 6-phosphate is added to the crystallization mixture, the enzyme shows bound gluose 6-phosphate at its active site in the crystals
P13377
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
unstable
6
-
-
immobilized enzyme: no marked change in the first few hours at different pH levels from pH 6.0-9.0, after a longer incubation the highest stability is measured at pH 6.0
7
-
-
stable
8
-
-
highest stability of soluble enzyme
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
-
15 min, stable
45
-
-
soluble enzyme, t1/2: 42 min. Immobilized enzyme, t1/2: 82 min
45
-
-
15 min, enzyme form PGI I, 50% loss of activity
50
-
-
soluble enzyme, t1/2: 12 min. Immobilized enzyme, t1/2: 10 min
50
-
-
30 min, no loss of activity
55
-
-
soluble enzyme, t1/2: 2 min. Immobilized enzyme, t1/2: 1 min
55
-
-
15 min, 50% loss of activity
55
-
-
15 min, complete loss of activity; 50% loss of activity, enzyme form PGI II
55
-
-
30 min, complete inactivation
55
-
-
stable up to
58
-
-
melting temperature
60
-
-
15 min, 90% loss of activity
60
-
-
free phosphoglucose isomerase is stable at a high protein concentration of 0.1 g/l (half-life of 180 h at 60C) but deactivates rapidly at low concentrations (half-life at 60C is 2.4 h at 0.001 g/l). Immobilized cellulose-binding module-phosphoglucose isomerase at a low concentration of 0.001 g/l has a half-life of 190 h, approximately 80fold of that of free phosphoglucose isomerase. Immobilized cellulose-binding module-phosphoglucose isomerase on regenerated amorphous cellulose is extremely stable at about 60C, nearly independent of its mass concentration in bulk solution
64
-
-
melting temperature
65
-
-
25% loss of activity after 1 h
65
-
-
purified native enzyme, half-life is 170 h
70
-
-
pH 7.0, 180 min, about 10% loss of activity
70
-
-
purified native enzyme, half-life is 68 h
75
-
-
purified native enzyme, half-life is 41 h
77
-
-, O28778
Tm-value of mutant enzyme G79L
80
-
-
120 min, stable
80
-
-
pH 7.0, 180 min, about 20% loss of activity
80
-
-
purified native enzyme, half-life is 25 h
85
-
-
purified native enzyme, half-life is 19 h
86
-
Q9HIC2, -
melting temperature
87
-
-, O28778
Tm-value of mutant enzyme G79A
90
-
-
120 min, about 40% loss of activity
90
-
-
pH 7.0, 180 min, about 50% loss of activity
90
-
-
half-life: 2.4 h
90
-
-
purified native enzyme, half-life is 11 h
95
-
-
120 min, about 90% loss of activity
95
-
-
purified native enzyme, half-life is 7.9 h
97
-
-, O28778
Tm-value of mutant enzyme H136A
98
-
-, O28778
Tm-value of wild-type enzyme and mutant enzymes T63A, H80A, H80D, H82A, E93A, E93D, Y95K and Y160F
100
-
-
3 min, complete loss of activity
100
-
-
pH 7.0, 180 min, about 60% loss of activity
100
-
-
melting temperature for thermal unfolding, 60 min, 50% residual activity
100
-
-, Q9YE01
melting temperature above 100C
additional information
-
-
thermal inactivation follows first-order kinetics
additional information
-
P06744
thermoinactivation of GPI genetic variants, overview
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the most basic of the five isoenzymes is more stable than the more acidic isoenzymes at pH extremes, at high ionic strength, in the presence of denaturants, or upon exposure to proteases
-
phosphoglucose isomerase in Tris-HCl buffer has 30% lower observed activity than that in the HEPES buffer at pH 7.0. At working conditions (100 mM HEPES buffer (pH 7.5) containing 10 mM Mg2+ and 0.5 mM Mn2+ at 60C), no significant activity is lost after 50 washings of immobilized cellulose-binding module-phosphoglucose isomerase
-
immobilization increases the stability against urea
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
susceptible to oxidation of sulfhydryl groups yielding multiple electrophoretic forms with catalytic activity
-
2838
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C or -20C, 20 mM Tris-acetate buffer, pH 8.0, stable for 1 month
-
best storage conditions: as crystalline suspension or precipitate in 0.70 saturated ammonium sulfate containing 50 mM triethanolamine buffer, pH 8.3, 1 mM EDTA, 1 mM dithiothreitol
-
-10C, in magnesium acetate solution, stable for several weeks
-
8-10C, storage stability of enzyme immobilized on different carriers, overview
-
4C, crystalline enzyme, 50% loss of activity after 5 months
-
4C, stable for more than 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
5 isoenzymes
-
native enzyme 468fold from skeletal muscle to homogeneity by ammonium sulfate fractionation, anion exchange and cation exchange chromatography, followed by gel filtration
-
affinity adsorption on regenerated amorphous cellulose and intein cleavage or ethylene glycol elusion method
-
affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
2 forms: low-molecular weight form PGI I, and high-molecular weight form PGI II
-
3 enzyme forms: isomerase a, b, and c
-
enzyme variants A, B and C
-
multiple forms: A, B and C
-
affinity chromatography
-
Ni-NTA column chromatography
-, P64192
overexpression in Escherichia coli
-
recombinant enzyme with His-tag. Rapid purification by Ni-NTA affinity chromatography with 80% yield
-
recombinant protein
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration to homogeneity
-
native enzyme 20fold by heat treatment and anion exchange chromatography
-
3 isoenzymes: A, B and C
-
cytosolic and stromal isoenzyme
-
cytosolic isoenzyme
-
cytosolic isoenzyme; plastid isoenzyme
-
2 enzyme forms PGI I and PGI II
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by immobilized metal ion affinity chromatography
P13377
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Agrobacterium tumefaciens
P34795
DNA and amino acid sequence determination, PGI genotyping for polymorphisms, influence of environmental conditions and geographic genetic structuring, modeling, overview
-
genotyping and polymorphisms, overview
-
expressed in Escherichia coli BL21 Star (DE3) cells
-
genotyping and polymorphisms, overview
-
DNA and amino acid sequence determination and analysis, GPI expression analysis, recombinant expression of the enzyme in Escherichia coli strain BL21
-
GPI gene, DNA and amino acid sequence determination and analysis, phylogenetic tree and expression analysis by real time quantitative RT-PCR, recombinant expression of His-tagged enzyme in Escherichia coli
-
DNA and amino acid sequence determination and analysis, sequence comparisons, phylogeneitic analysis, and genotyping for polymorphisms
C8TDU8, -
isozyme A and B overexpressed in Escherichia coli
-
expression analysis
-
expression of wild-type and mutant enzymes in Escherichia coli strain DF2145
P06744
native enzyme and mutant enzymes T5I, T224M, Q343R, D539N
-
PGI, expression analysis in cells from healthy and colon cancer individuals
-
genotyping and polymorphisms, overview
-
expression in Escherichia coli
-
expression in Escherichia coli
-
overexpression of His-tagged enzyme in Escherichia coli strain BL21 (DE3)
-
expression in Escherichia coli BL21
-
overexpressed in Escherichia coli
-
overexpression in Escherichia coli
-
overexpression in Escherichia coli
P84140, -
expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
P13377
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
GPI is induced up to eightfold by 2.5 M and 14fold higher by 3.5 M NaCl compared to activity at 1.5 M NaCl, respectively
-
GPI is induced up to eightfold by 2.5 M and 14fold higher by 3.5 M NaCl compared to activity at 1.5 M NaCl, respectively; GPI is induced up to eightfold by 2.5 M and 14fold higher by 3.5 M NaCl compared to activity at 1.5 M NaCl, respectively
Dunaliella salina UTEX-LB-1644
-
-
alpha-phosphoglucomutase overexpression in strain BL311 leads to diminished levels of Pgi activity
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E93A
-, O28778
Ni2+ content and apparent Ni2+ binding ability is reduced
E93D
-, O28778
catalytic efficiency is reduced by more than 100fold. Ni2+ content and apparent Ni2+ binding ability is reduced
G79A
-, O28778
mutant enzyme exhibits a lower thermostability, catalytic efficiency is reduced by more than 100fold
G79L
-, O28778
mutant enzyme exhibits a lower thermostability, catalytic efficiency is reduced by more than 100fold
H136A
-, O28778
catalytic efficiency remains about the same compared to wild-type activity
H80A
-, O28778
catalytic efficiency is reduced by more than 100fold. Ni2+ content and apparent Ni2+ binding ability is reduced
H80D
-, O28778
catalytic efficiency is reduced by more than 100fold. Ni2+ content and apparent Ni2+ binding ability is reduced
H82A
-, O28778
catalytic efficiency is reduced by more than 15fold, catalytic efficiency is reduced by more than 15fold. Ni2+ content and apparent Ni2+ binding ability is reduced
T63A
-, O28778
catalytic efficiency is reduced by more than 15fold
Y160F
-, O28778
catalytic efficiency is reduced by more than 15fold
Y95F
-, O28778
mutant enzyme exhibits a lower thermostability, catalytic efficiency is reduced by more than 100fold
Y95K
-, O28778
catalytic efficiency is reduced by more than 15fold
A300P
P06744
the mutation may affect the folding efficiency of the enzyme protein, the mutant shows reduced expression level and barely detectable activity
A346H
-
mutation identified in a patient suffering from chronic nonspherocytic hemolytic anemia. Loss of 82% of enzyme activity, loss of enzyme capability to dimerize. Mutation results in significant changes in erythrocyte metabolism
E495K
P06744
the mutation may affect the folding efficiency of the enzyme protein, the mutant shows reduced expression level and barely detectable activity; the mutation weakens network bonding of the enzyme
H389R
P06744
the mutation at or near the active site highly affects the catalytic efficiency of the enzyme, the mutant shows barely detectable activity
I525T
P06744
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency; the mutation destabilizes the ternary structure of the enzyme
L339P
P06744
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency; the mutation may affect the folding efficiency of the enzyme protein, the mutant shows reduced expression level and barely detectable activity
Q343R
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
R273H
P06744
the mutation at or near the active site highly affects the catalytic efficiency of the enzyme, the mutant shows barely detectable activity
R347C
P06744
the mutation destabilizes the ternary structure of the enzyme; the mutation weakens network bonding of the enzyme
R347H
P06744
the mutation destabilizes the ternary structure of the enzyme; the mutation weakens network bonding of the enzyme
R472H
P06744
the mutation weakens network bonding of the enzyme
R539N
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
R75G
P06744
the mutation weakens network bonding of the enzyme
R83W
P06744
the mutation increases the water-accessible hydrophobic surface
S278L
P06744
the mutation at or near the active site highly affects the catalytic efficiency of the enzyme; the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
T195I
P06744
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency; the mutation destabilizes the ternary structure of the enzyme
T224M
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
T375R
P06744
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
T5I
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
V101M
P06744
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
T211A
-, P64192
the mutant shows decreased activity with higher Km compared with that of the wild type protein
E98V
P84140, -
the ratio of turnover number and Km-value is 31373fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
H137A
P84140, -
the ratio of turnover number and Km-value is 66.7fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
H89A
P84140, -
the ratio of turnover number and Km-value is 2712fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
H91A
P84140, -
the ratio of turnover number and Km-value is 66.7fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
G189E
-
GroD1 enzyme mutant cells show 87% reduced enzyme activity and defects in glycerolipid biosynthesis, overview. The phenotype comprises profound reduction in the synthesis of phosphatidylcholine, phosphatidylethanolamine, and triglycerides but high levels of phosphatidic acid and normal levels of phosphatidylinositol synthesis, accompanied by a reduction in phosphatidate phosphatase 1 activity. Expression of wild-type hamster GPI restores GPI activity, glycerolipid biosynthesis, and PAP1 activity in GroD1
additional information
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independently isolated GPI-deficient mutants displayed similar phenotypes like G189E with respect to PAP1 activity and glycerolipid biosynthesis
additional information
C8TDU8, -
identification of 33 single nucleotide polymorphisms and 14 insertion/deletion sites in the strain and EtG6-PI coding sequence
additional information
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mutant with point mutation in enzyme gene shows abnormal development after germination by extending a primary germ tube that quickly reverts to siotropic growth and results in an enlarged, swollen apex with pronounced wall thickenings. Mutant is unable to conidiate due to a block in conidiophore development at vesicle formation
L487F
P06744
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
additional information
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downregulation of enzyme expression by siRNA results in increased sensitivity to oxidative stress and oxidative stress-induced cellular senescence. The senscence pathway involving p21 cyclin-dependent kinase inhibitor is up-regulated in enzyme knock-down cells
additional information
P06744
thermoinactivation of GPI genetic variants, phenotypes, overview
additional information
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ectopic expression of PGI/AMF induces epithelial-to-mesenchymal transition in MCF10A epithelial breast cancer cells. Inhibition of PGI/AMF expression triggers mesenchymal-to-epithelial transition in aggressive mesenchymal-type breast cancer MD-MB-231 cells
G157Y
-, P64192
the mutation results in a complete loss of activity
additional information
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recombinant enzyme carrying His-tag shows enzymatic acitivity equal to native enzyme
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
activity of EDTA-inhibited enzyme is completely restored by addition of manganese
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enzyme inactivated by 100fold excess of EDTA can be reactivated by 1000fold excess of of Zn2+
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after dissociation the enzyme can readily by reassociated and renatured with a yield of maximal 73% and a pseudo first order rate constant of 0.12 per min at 25C
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
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phosphoglucose isomerase variability of Cerastoderma glaucum as a model for testing the influence of environmental conditions and dispersal patterns through quantitative ecology approaches, overview. The PGI locus is an appropriate marker for revealing the spatial distribution of genetic variation and for establishing the relationships between allelic composition and the environmental influencing variables
analysis
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Pgi is an adaptive marker, rather than providing insights into individual genetic health, Pgi appears to have a role in conservation genetics by providing insights into gene by environment interactions, local adaptation and evolutionary significant units, and potentially even morphologically cryptic dispersal phenotypes, method development, overview
drug development
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the enzyme is a target for development of specific inhibitors against Echinococcus multilocularismetacestodes and disease alveolar echinococcosis, overview
drug development
C8TDU8, -
the enzyme is a valid drug target against protozoa in coccidiosis
medicine
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use as a diagnostic tool in medicine
medicine
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frequency of enzyme variants in healthy control subjects with anti-glucoes 6-phosphate antibodies is significantly higher than in antibody-negative healthy subjects. Frequency of enzyme variants in anti-glucose 6-phosphate antibody positive patients suffering from rheumatoid arthritis is more significantly higher than in antibody-negative patients
medicine
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mutation A346H is identified in a patient suffering fromchronic nonspherocytic hemolytic anemia. Mutation results in loss of 82% of enzyme activity, loss of enzyme capability to dimerize, and in significant changes in erythrocyte metabolism
medicine
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sera and synovial fluids from patients with immune-based inflammatory arthritis contain significantly higher levels of enzyme activity and of enzyme protein both in inactive and active form than healthy control or patients with non-immune based inflammatory arthritis
medicine
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enzyme expression is detected in a major proportion of lung carcinomas, and enzyme may play a part in proliferation and/or progression of the tumours as well as possibly in the differentiation of squamous cell carcinoma. higher enzyme mRNA expression may be related to the high metastatic potential of non-small cell lung carcinomas and to increased protein secretion
analysis
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Pgi is an adaptive marker, rather than providing insights into individual genetic health, Pgi appears to have a role in conservation genetics by providing insights into gene by environment interactions, local adaptation and evolutionary significant units, and potentially even morphologically cryptic dispersal phenotypes, method development, overview
drug development
P13377
PGI might be a good target for species-specific drug design
drug development
Trypanosoma brucei Treu 927
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PGI might be a good target for species-specific drug design
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