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Information on EC 5.4.2.8 - phosphomannomutase and Organism(s) Pseudomonas aeruginosa and UniProt Accession P26276
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5.4.2.8 phosphomannomutaseIUBMB Comments
alpha-D-Mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor.
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Word Map
- 5.4.2.8
-
carbohydrate-deficient
- transferrin
- gdp-mannose
-
multisystemic
-
cdg-ia
-
team
- mannose-1-phosphate
-
pectoralis
- phosphoglucomutase
-
doctors
-
obstetric
-
hypoglycosylation
-
nipple
-
lipid-linked
-
psoas
-
premammillary
-
strabismus
- paromomycin
-
meniscectomy
- medicine
- food industry
- biotechnology
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
pmm, phosphomannomutase, orf17, phosphomannomutase 2, phosphomannomutase2, alpha-d-phosphohexomutase, phosphomannose mutase, alpha-phosphomannomutase1, pmm-1, pmm-2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PMM/PGM
ORF17
-
-
-
-
Phosphomannose mutase
-
-
-
-
Phosphomutase, mannose
-
-
-
-
PMM
-
-
-
-
PMM/PGM
PMMH-22
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-D-glucose 1-phosphate = D-glucose 6-phosphate
acid-base catalysis mechanism, key role for conformational change in its multistep reaction, which requires a dramatic 180 degree reorientation of the intermediate within the active site. Modeling shows that increased enzyme flexibility facilitates the reorientation of the reaction intermediate, coupling changes in structural dynamics with the unique catalytic mechanism of this enzyme
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
alpha-D-mannose 1,6-phosphomutase
alpha-D-Mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor.
CAS REGISTRY NUMBER
COMMENTARY
59536-73-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-mannose 6-phosphate
D-mannose 1-phosphate
-
the enzyme is required for synthesis of lipopolysaccharide O side chains
-
-
?
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase, EC 5.4.2.2, and phosphomannomutase activities
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
PMM/PGM catalyzes the second step in alginate biosynthesis
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
second step of the alginate biosynthetic pathway
-
r
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
more slowly in the reverse direction
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
PMM/PGM catalyzes the second step in alginate biosynthesis
-
r
D-mannose 6-phosphate
D-mannose 1-phosphate
-
the enzyme is required for synthesis of lipopolysaccharide O side chains
-
-
?
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase, EC 5.4.2.2, and phosphomannomutase activities
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
second step of the alginate biosynthetic pathway
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Disperse Blue 56
-
kinetic studies indicate that it is a parabolic, noncompetitive inhibitor. Reduction of the inhibition in the presence of 0.01% Triton X-100
additional information
-
not inhibitory: 1,5-diamino-4,8-dihydroxyanthraquinone
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0272
alpha-D-glucose 1-phosphate
wild type enzyme, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0354
alpha-D-glucose 1-phosphate
mutant enzyme P368A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0366
alpha-D-glucose 1-phosphate
mutant enzyme S369A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0489
alpha-D-glucose 1-phosphate
mutant enzyme P368G, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0491
alpha-D-glucose 1-phosphate
mutant enzyme R262A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0493
alpha-D-glucose 1-phosphate
mutant enzyme Y17A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0518
alpha-D-glucose 1-phosphate
mutant enzyme E325A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0667
alpha-D-glucose 1-phosphate
mutant enzyme R262A/P368G, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.012
alpha-D-glucose 1-phosphate
mutant enzyme E325A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.05
alpha-D-glucose 1-phosphate
mutant enzyme Y17A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.48
alpha-D-glucose 1-phosphate
mutant enzyme R262A/P368G, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.87
alpha-D-glucose 1-phosphate
mutant enzyme R262A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
1.02
alpha-D-glucose 1-phosphate
mutant enzyme P368A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
1.23
alpha-D-glucose 1-phosphate
mutant enzyme P368G, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
2.17
alpha-D-glucose 1-phosphate
mutant enzyme S369A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
7.83
alpha-D-glucose 1-phosphate
wild type enzyme, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the enzyme catalyzes an intramolecular phosphoryl transfer across its phosphosugar substrates, which are precursors in the synthesis of exoproducts involved in bacterial virulence
additional information
-
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
structure analysis of the active phosphoenzyme, the inactive dephosphoenzyme, and the phosphoenzyme in complex with the substrate analog xylose 1-phosphate, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
phosphoprotein
active form of PMM/PGM is phosphorylated at Ser108
phosphoprotein
the enzyme requires conserved phosphoserine 108 for activity
phosphoprotein
-
mutation of serine 108 where phosphorylation occurs results in phosphorylation of a different residue, so that activity is reduced only 20fold from that of wild-type
phosphoprotein
-
phosphorylation of conserved catalytic active site residue Ser108 has broad effects on residues in multiple domains. Dephosphorylation of the enzyme may play two critical functional roles: a direct role in the chemical step of phosphoryl transfer and secondly through propagation of structural flexibility. Dephosphorylation has minimal effects on crystal structure of the enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the selenomethionine-substituted PMM/PGM at 2.2 A resolution, crystal structure of S108A mutant at 1.75 A resolution
12-15 mg/ml PMM/PGM solution in 10 mM MOPS, crystals grow by hanging-drop vapor diffusion from 1.4 M sodium/potassium tartrate and 100 mM Na-HEPES, pH 7.5 from drops containing 0.002 ml protein and 0.002 ml of well buffer, crystals diffract to 1.75 A
-
in complex with inhibitor xylose 1-phosphate or slow substrate ribose 1-phosphate. Both ligands induce an interdomain rearrangement, using different enzyme-ligand interactions
-
phospho- and dephospho-enzyme in complex with reaction intermediate glucose 1,6-bisphosphate at 1.9 and 2.0 A
-
purified recombinant detagged enzyme, hanging drop vapor diffusion and microseeding techniques, 1.3 to 1.4 M sodium/potassium tartrate and 100 mM HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N110A
-
no remarkable differences in Km and Vmax value compared to wild-type, but intermediate glucose-1,6-bisphosphate dissociates from mutant 25times more often than from wild-type
R15A
-
no remarkable differences in Km and Vmax value compared to wild-type, but intermediate glucose-1,6-bisphosphate dissociates from mutant 25times more often than from wild-type
R247A
-
no remarkable differences in Km and Vmax value compared to wild-type, modest increase in dissociation of intermediate glucose-1,6-bisphosphate from enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3), removal of the His-tag, purification by nickel affinity chromatography and dialysis
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
nucleotide sequence of wild-type and mutant algC genes as well as the transcription and translational initiation sites of the wild-type gene
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Padgett, P.J.; Phibbs, P.V.
Phosphomannomutase activity in wild-type and alginate-producing strains of Pseudomonas aeruginosa
Curr. Microbiol.
14
187-192
1986
Pseudomonas aeruginosa
-
Sa-Correia, I.; Darzins, A.; Wang, S.K.; Berry, A.; Chakrabarty, A.M.
Alginate biosynthetic enzymes in mucoid and nonmucoid Pseudomonas aeruginosa: overproduction of phosphomannose isomerase, phosphomannomutase, and GDP-mannose pyrophosphorylase by overexpression of the phosphomannose isomerase (pmi) gene
J. Bacteriol.
169
3224-3231
1987
Pseudomonas aeruginosa
Goldberg, J.B.; Hatano, K.; Pier, G.B.
Synthesis of lipopolysaccharide O side chains by Pseudomonas aeruginosa PAO1 requires the enzyme phosphomannomutase
J. Bacteriol.
175
1605-1611
1993
Pseudomonas aeruginosa
Zielinski, N.A.; Chakrabarty, A.M.; Berry, A.
Characterization and regulation of the Pseudomonas aeruginosa algC gene encoding phosphomannomutase
J. Biol. Chem.
266
9754-9763
1991
Pseudomonas aeruginosa
Regni, C.A.; Tipton, P.A.; Beamer, L.J.
Crystallization and initial crystallographic analysis of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa
Acta Crystallogr. Sect. D
56
761-762
2000
Pseudomonas aeruginosa
Naught, L.E.; Tipton, P.A.
Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase
Arch. Biochem. Biophys.
396
111-118
2001
Pseudomonas aeruginosa
Naught, L.E.; Regni, C.; Beamer, L.J.; Tipton, P.A.
Roles of active site residues in Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase
Biochemistry
42
9946-9951
2003
Pseudomonas aeruginosa (P26276)
Regni, C.; Tipton, P.A.; Beamer, L.J.
Crystal Structure of PMM/PGM: An Enzyme in the Biosynthetic Pathway of P. aeruginosa Virulence Factors
Structure
10
269-279
2002
Pseudomonas aeruginosa (P26276)
Liu, H.Y.; Wang, Z.; Regni, C.; Zou, X.; Tipton, P.A.
Detailed kinetic studies of an aggregating inhibitor; inhibition of phosphomannomutase/phosphoglucomutase by disperse blue 56
Biochemistry
43
8662-8669
2004
Pseudomonas aeruginosa
Regni, C.; Shackelford, G.S.; Beamer, L.J.
Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor
Acta Crystallogr. Sect. F
F62
722-726
2006
Pseudomonas aeruginosa
Regni, C.; Schramm, A.M.; Beamer, L.J.
The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme
J. Biol. Chem.
281
15564-15571
2006
Pseudomonas aeruginosa
Schramm, A.M.; Mehra-Chaudhary, R.; Furdui, C.M.; Beamer, L.J.
Backbone flexibility, conformational change, and catalysis in a phosphohexomutase from Pseudomonas aeruginosa
Biochemistry
47
9154-9162
2008
Pseudomonas aeruginosa (P26276)
Lee, Y.; Villar, M.T.; Artigues, A.; Beamer, L.J.
Promotion of enzyme flexibility by dephosphorylation and coupling to the catalytic mechanism of a phosphohexomutase
J. Biol. Chem.
289
4674-4682
2014
Pseudomonas aeruginosa
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