Information on EC 5.4.2.2 - phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) and Organism(s) Homo sapiens

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Homo sapiens


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


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
5.4.2.2
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RECOMMENDED NAME
GeneOntology No.
phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent)
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-galactose degradation I (Leloir pathway)
-
-
D-galactose degradation V (Leloir pathway)
-
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GDP-glucose biosynthesis
-
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glucose and glucose-1-phosphate degradation
-
-
glucosylglycerol biosynthesis
-
-
glycogen biosynthesis I (from ADP-D-Glucose)
-
-
glycogen biosynthesis III (from alpha-maltose 1-phosphate)
-
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glycogen degradation I
-
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glycogen degradation II
-
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starch biosynthesis
-
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starch degradation III
-
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starch degradation V
-
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streptomycin biosynthesis
-
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sucrose biosynthesis II
-
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sucrose degradation II (sucrose synthase)
-
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sucrose degradation IV (sucrose phosphorylase)
-
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trehalose degradation V
-
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UDP-alpha-D-glucose biosynthesis I
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degradation of hexoses
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glycogen metabolism
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Glycolysis / Gluconeogenesis
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Pentose phosphate pathway
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Galactose metabolism
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Purine metabolism
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Starch and sucrose metabolism
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Amino sugar and nucleotide sugar metabolism
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Streptomycin biosynthesis
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucose 1,6-phosphomutase
Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. The enzyme also catalyses (more slowly) the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. cf. EC 5.4.2.5, phosphoglucomutase (glucose-cofactor).
CAS REGISTRY NUMBER
COMMENTARY hide
9001-81-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
-
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-bisphosphoglycerate
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fructose 1,6-diphosphate
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-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-D-glucose 1,6-diphosphate
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Km: 0.00077-0.00163 mM
cysteine
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required
GSH
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required
histidine
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required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.057 - 0.088
glucose 1-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40.2
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isozyme PGM2, substrate glucose 1-phosphate
42
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isozyme PGM2, substrate glucose 1-phosphate
1263
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isozyme PGM1, substrate glucose 1-phosphate
1442
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isozyme PGM1, substrate glucose 1-phosphate
additional information
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assay method for serum
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 7.6
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8
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isozymes PGM1 and PGM2
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
inhibition of phosphoglucomutase activity by chronic treatment with Li+ causes compensatory elevation of phosphoglucomutase activity in Li+-treated bipolar patients due to increased expression of PGM1 gene
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58500
-
isozyme PGM1, gel filtration, SDS-PAGE
69000
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isozyme PGM2, gel filtration, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 58500, isozyme PGM1, SDS-PAGE; 1 * 69000, isozyme PGM1, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isozymes PGM1 and PGM2
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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inhibition of phosphoglucomutase activity by chronic treatment with Li+ causes compensatory elevation of phosphoglucomutase activity in Li+-treated bipolar patients due to increased expression of PGM1 gene