5.4.2.2: phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent)
This is an abbreviated version!
For detailed information about phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent), go to the full flat file.
Word Map on EC 5.4.2.2
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5.4.2.2
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starch
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hexokinase
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glycogen
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malate
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phosphorylase
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6-phosphogluconate
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pyrophosphorylase
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1-phosphate
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adenylate
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esterase
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erythrocyte
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galactose
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glucose-1-phosphate
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aldolase
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phosphofructokinase
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transferrin
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gpi
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allozyme
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haptoglobin
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malic
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glucosephosphate
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zymodemes
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histolytica
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hardy-weinberg
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entamoeba
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glyoxalase
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adp-glucose
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phosphoglucoisomerase
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glucose-6-phosphatase
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monomorphic
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plastidial
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glycogenolysis
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fructokinase
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diptera
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galactose-1-phosphate
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phosphohexose
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starch-gel
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uridylyltransferase
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5.3.1.9
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glc-6-p
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bloodstain
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udp-galactose
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leloir
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amyloplasts
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duffy
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udp-glc
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phosphoenzyme
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isoenzymatic
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2.7.1.1
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1,6-diphosphate
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drug development
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molecular biology
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food industry
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medicine
- 5.4.2.2
- starch
- hexokinase
- glycogen
- malate
- phosphorylase
- 6-phosphogluconate
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pyrophosphorylase
- 1-phosphate
- adenylate
- esterase
- erythrocyte
- galactose
- glucose-1-phosphate
- aldolase
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phosphofructokinase
- transferrin
- gpi
-
allozyme
- haptoglobin
-
malic
-
glucosephosphate
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zymodemes
- histolytica
-
hardy-weinberg
- entamoeba
- glyoxalase
- adp-glucose
- phosphoglucoisomerase
- glucose-6-phosphatase
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monomorphic
- plastidial
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glycogenolysis
- fructokinase
- diptera
- galactose-1-phosphate
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phosphohexose
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starch-gel
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uridylyltransferase
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5.3.1.9
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glc-6-p
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bloodstain
- udp-galactose
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leloir
- amyloplasts
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duffy
- udp-glc
- phosphoenzyme
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isoenzymatic
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2.7.1.1
- 1,6-diphosphate
- drug development
- molecular biology
- food industry
- medicine
Reaction
Synonyms
alpha phosphoglucomutase, alpha-Pgm, alpha-phosphoglucomutase, alpha-phosphoglucomutase 1, alpha-phosphoglucose mutase, cPGM, cytosolic phosphoglucomutase, EC 2.7.5.1, Glucose phosphomutase, PGM, PGM-I, PGM-II, PGM/PMM, PGM1, PGM2, PGM3, PgmA, PgmG, phospho-glucomutase, phosphoglucomutase, phosphoglucomutase 1, phosphoglucomutase/phosphomannomutase, phosphoglucomutase1, Phosphoglucose mutase, Phosphohexomutase, phosphomannomutase/phosphoglucomutase, Phosphomutase, glucose, plastidic phosphoglucomutase, PMM/PGM, pPGM, SP-1, SpgM, SSO0207, XanA, YMR278w protein
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General Information
General Information on EC 5.4.2.2 - phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent)
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evolution
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the enzyme belongs to the alpha-D-phosphohexomutase enzyme superfamily
malfunction
metabolism
physiological function
additional information
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targeted deletion of pgmA in Yersinia pestis strain KIM5 results in loss of autoaggregation, the deletion mutant displays more than 1000fold increased sensitivity to polymyxin B compared to the parental strain
malfunction
the pgm deletion mutant has impaired growth in vitro, is deficient in the ability to utilize alpha-D-galactose as a carbon source and displays reduced O-antigen polymer length
malfunction
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whereas pgm2 and pgm3 single mutants are undistinguishable from the wild type, loss of both PGM2 and PGM3 severely impairs male and female gametophyte function. Double mutant pollen completes development but fails to germinate, double mutant ovules also develop normally, but approximately half remain unfertilized 2 d after pollination
malfunction
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only mutants with a deletion of PGM3, not of PGM1 or PGM2, hyperaccumulate ribose-1-phosphate
malfunction
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an enzyme-deficient mutant shows significantly reduced survival in embryonic trophoblast cells and in mice, and induces high protective immunity in BALB/c mice. Moreover, the mutant elicits an anti-Brucella-specific immunoglobulin G response and induces the secretion of gamma interferon and interleukin-2
malfunction
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complete enzyme loss results in dwarf growth, prematurely die off, and inability to develop a functional inflorescence
malfunction
enzyme depletion is associated with declined cellular glycogen content and decreased rates of glycogenolysis and glycogenesis. Furthermore, enzyme depletion suppresses cell proliferation under long-term repetitive glucose depletion
malfunction
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whereas pgm2 and pgm3 single mutants are undistinguishable from the wild type, loss of both PGM2 and PGM3 severely impairs male and female gametophyte function. Double mutant pollen completes development but fails to germinate, double mutant ovules also develop normally, but approximately half remain unfertilized 2 d after pollination
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malfunction
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an enzyme-deficient mutant shows significantly reduced survival in embryonic trophoblast cells and in mice, and induces high protective immunity in BALB/c mice. Moreover, the mutant elicits an anti-Brucella-specific immunoglobulin G response and induces the secretion of gamma interferon and interleukin-2
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malfunction
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targeted deletion of pgmA in Yersinia pestis strain KIM5 results in loss of autoaggregation, the deletion mutant displays more than 1000fold increased sensitivity to polymyxin B compared to the parental strain
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malfunction
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the pgm deletion mutant has impaired growth in vitro, is deficient in the ability to utilize alpha-D-galactose as a carbon source and displays reduced O-antigen polymer length
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cytosolic PGM activity is not limiting for carbon metabolism
metabolism
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PGM is a key enzyme in carbohydrate metabolism, where it catalyzes the reversible transfer of a phosphate group between C-1 and C-6 of D-glucose via D-glucose 1,6-diphosphate
metabolism
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PGM is a key enzyme in carbohydrate metabolism, where it catalyzes the reversible transfer of a phosphate group between C-1 and C-6 of D-glucose via D-glucose 1,6-diphosphate
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metabolism
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cytosolic PGM activity is not limiting for carbon metabolism
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Pgm is required by Salmonella enterica serovar Typhimurium for O-antigen production, resistance to antimicrobial peptides, and in vivo fitness
physiological function
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PgmA is required for efficient autoaggregation in Yersinia pestis and plays an important role in antimicrobial peptide resistance
physiological function
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overexpression of pgm gene has no significant effect on UDP-glucose and UDP-galactose levels and increased alpha-Pgm activity does not significantly change the lactate production
physiological function
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pollen germination requires cytosolic PGM activity
physiological function
Unlike the majority of alpha-phosphoglucomutases, the described enzyme of 252 residues with alpha-phosphoglucomutase activity, is related to eukaryotic phosphomannomutases and belongs to HAD-superfamily hydrolase, subfamily IIB.
physiological function
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the enzyme catalyzes an intramolecular phosphoryl transfer across its phosphosugar substrates, which are precursors in the synthesis of exoproducts involved in bacterial virulence
physiological function
the enzyme is involved in biosynthesis of sphingans, extracellular polysaccharides
physiological function
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the enzyme is involved in glycogen catabolism
physiological function
the enzyme plays an important role in polysaccharide capsule formation and virulence in a number of bacterial pathogens
physiological function
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the plastidial PGM limits photosynthetic carbon flow into starch
physiological function
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the enzyme is essential for glucose phosphate partitioning and, therefore, for syntheses of sucrose and cell wall components
physiological function
the enzyme is necessary for sustained cell growth under repetitive glucose depletion
physiological function
the enzyme is required for hyphal growth, polysaccharide production, and cell wall integrity
physiological function
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pollen germination requires cytosolic PGM activity
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physiological function
Ganoderma lucidum ACCC 53264
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the enzyme is required for hyphal growth, polysaccharide production, and cell wall integrity
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physiological function
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PgmA is required for efficient autoaggregation in Yersinia pestis and plays an important role in antimicrobial peptide resistance
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physiological function
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Pgm is required by Salmonella enterica serovar Typhimurium for O-antigen production, resistance to antimicrobial peptides, and in vivo fitness
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physiological function
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the enzyme plays an important role in polysaccharide capsule formation and virulence in a number of bacterial pathogens
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physiological function
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the enzyme is involved in biosynthesis of sphingans, extracellular polysaccharides
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analysis of conformational flexibility of different forms of phosphoglucomutase/phosphomannomutase in solution, including its active, phosphorylated state and the unphosphorylated state that occurs transiently during the catalytic cycle, by hydrogen-deuterium exchange by mass spectrometry and small angle x-ray scattering. Both ligand binding and phosphorylation of the catalytic phosphoserine affect the overall flexibility of the enzyme in solution
additional information
structure homology modeling, overview