Information on EC 2.7.1.106 - glucose-1,6-bisphosphate synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.106
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RECOMMENDED NAME
GeneOntology No.
glucose-1,6-bisphosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-phospho-D-glyceroyl phosphate + alpha-D-glucose 1-phosphate = 3-phospho-D-glycerate + alpha-D-glucose 1,6-bisphosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Starch and sucrose metabolism
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SYSTEMATIC NAME
IUBMB Comments
3-phospho-D-glyceroyl-phosphate:alpha-D-glucose-1-phosphate 6-phosphotransferase
D-Glucose 6-phosphate can act as acceptor, forming alpha-D-glucose 1,6-bisphosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
56214-39-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-phospho-D-glyceroyl phosphate + D-glucose 1-phosphate
3-phospho-D-glycerate + D-glucose 1,6-bisphosphate
show the reaction diagram
3-phospho-D-glyceroyl phosphate + D-glucose 6-phosphate
3-phospho-D-glycerate + D-glucose 1,6-bisphosphate
show the reaction diagram
3-phospho-D-glyceroyl phosphate + D-mannose 1-phosphate
3-phospho-D-glycerate + D-mannose 1,6-bisphosphate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-phospho-D-glyceroyl phosphate + D-glucose 1-phosphate
3-phospho-D-glycerate + D-glucose 1,6-bisphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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requirement, can be replaced by Mg2+, Mn2+, Zn2+, Ni2+, Co2+, Cd2+
Cd2+
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requirement, can be replaced by Mg2+, Mn2+, Ca2+, Zn2+, Ni2+, Co2+
Mn2+
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requirement, can be replaced by Mg2+, Ca2+, Zn2+, Ni2+, Co2+, Cd2+
Ni2+
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requirement, can be replaced by Mg2+, Mn2+, Ca2+, Zn2+, Co2+, Cd2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-bisphosphoglycerate
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0.2 mM, strong inhibitor
acetyl-CoA
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cis/trans-aconitate
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citrate
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D-fructose 1,6-diphosphate
D-Glucose 1,6-bisphosphate
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0.01 mM, 50% inhibition
D-glucose 1,6-diphosphate
Glutarate
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weak
glycerate 2,3-diphosphate
Glycerate 3-phosphate
glycerol 3-phosphate
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; 0.2 mM, strong inhibitor
Imidazole/EDTA
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isocitrate
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K+
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weak
L-malate
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weak
Li+
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strong, dilution, Co2+ or Zn2+ protects, not Ca2+, Mg2+ or Mn2+
Na+
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weak
phosphate
phosphoenolpyruvate
tricarballylate
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additional information
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no inhibition by adipate or succinate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000087 - 0.00045
3-phospho-D-glyceroyl 1-phosphate
0.009 - 0.16
D-glucose 1-phosphate
0.015 - 0.061
D-glucose 6-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0045
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liver enzyme
0.136
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erythrocyte enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 8.7
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about half-maximal activity at pH 7.3 and 8.7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
liver: 2 isozymes
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partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as fusion protein with a polyHis tag at their N-terminus
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