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Information on EC 5.3.1.9 - glucose-6-phosphate isomerase and Organism(s) Plasmodium falciparum

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IUBMB Comments
The enzyme from yeast catalyses the reversible conversion specifically between the alpha-D-glucose 6-phosphate and beta-D-fructofuranose 6-phosphate. The enzyme also catalyses the anomerization of both D-hexose 6-phosphates .
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This record set is specific for:
Plasmodium falciparum
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Word Map
The taxonomic range for the selected organisms is: Plasmodium falciparum
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphoglucose isomerase, glucose-6-phosphate isomerase, glucose phosphate isomerase, autocrine motility factor, phosphoglucoisomerase, phosphohexose isomerase, neuroleukin, pgi/amf, amf/pgi, glucose 6-phosphate isomerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6-Phosphoglucose isomerase
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-
-
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D-Glucose-6-phosphate isomerase
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-
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D-glucose-6-phosphate ketol-isomerase
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-
-
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Glucose 6-phosphate isomerase
Glucose phosphate isomerase
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-
-
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Glucose phosphoisomerase
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-
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Glucosephosphate isomerase 2
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-
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Hexose 6-phosphate isomerase
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-
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Hexose isomerase
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-
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Hexose monophosphate isomerase
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-
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Hexose phosphate isomerase
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-
-
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Hexosephosphate isomerase
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-
-
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Isomerase, glucose phosphate
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-
-
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Neuroleukin
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-
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NLK
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-
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Oxoisomerase
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-
-
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PGI2
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-
-
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PGI3
-
-
-
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Phosphoglucoisomerase
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-
-
-
Phosphoglucose isomerase
Phosphohexoisomerase
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-
-
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Phosphohexomutase
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-
-
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Phosphohexose isomerase
Phosphosaccharomutase
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-
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SA-36
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-
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Sperm antigen-36
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-
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VEG54
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-
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Vegetative protein 54
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
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-
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isomerization
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-
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucose-6-phosphate aldose-ketose-isomerase (configuration-inverting)
The enzyme from yeast catalyses the reversible conversion specifically between the alpha-D-glucose 6-phosphate and beta-D-fructofuranose 6-phosphate. The enzyme also catalyses the anomerization of both D-hexose 6-phosphates [7].
CAS REGISTRY NUMBER
COMMENTARY hide
9001-41-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
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-
-
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r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.228 - 0.278
fructose 6-phosphate
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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PGI is a key enzyme in glycolysis and glycogenesis catalyzing the second step of glycolysis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
G6PI_PLAFA
591
0
68766
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
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x * 65000, recombinant enzyme, SDS-PAGE
66000
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x * 66000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of His-tagged enzyme in Escherichia coli strain BL21 (DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Srivastava, I.K.; Schmidt, M.; Grall, M.; Certa, U.; Garcia, A.M.; Perrin, L.H.
Identification and purification of glucose phosphate isomerase of Plasmodium falciparum
Mol. Biochem. Parasitol.
54
153-164
1992
Plasmodium falciparum
Manually annotated by BRENDA team
Aoki, K.; Tanaka, N.; Kusakabe, Y.; Fukumi, C.; Haga, A.; Nakanishi, M.; Kitade, Y.; Nakamura, K.T.
Crystallization and preliminary X-ray crystallographic study of phosphoglucose isomerase from Plasmodium falciparum
Acta Crystallogr. Sect. F
66
333-336
2010
Plasmodium falciparum
Manually annotated by BRENDA team