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Synonyms
pmm, phosphomannomutase, orf17, phosphomannomutase 2, phosphomannomutase2, alpha-d-phosphohexomutase, phosphomannose mutase, alpha-phosphomannomutase1, pmm-1, pmm-2,
more
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alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
alpha-D-mannose-1-phosphate
D-mannose-6-phosphate
-
-
-
-
r
D-glucose-1-phosphate
D-glucose-6-phosphate
-
-
-
-
r
D-Mannose 1-phosphate
D-Mannose 6-phosphate
D-mannose 6-phosphate
D-mannose 1-phosphate
-
the enzyme is required for synthesis of lipopolysaccharide O side chains
-
-
?
Glucose 1-phosphate
Glucose 6-phosphate
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
r
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
more slowly in the reverse direction
-
?
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alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
r
alpha-D-glucose 1-phosphate
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
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
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
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0.0272 - 0.0667
alpha-D-glucose 1-phosphate
0.0013 - 0.016
glucose 1-phosphate
0.0127 - 0.0279
alpha-D-glucose 1-phosphate
0.06
mannose 1-phosphate
-
-
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
0.0013
glucose 1-phosphate
H308N/H329N double mutant
0.0013
glucose 1-phosphate
S108A mutant
0.0024
glucose 1-phosphate
S108A/H308N double mutant
0.0027
glucose 1-phosphate
K118L/H109Q double mutant
0.0028
glucose 1-phosphate
R20A mutant
0.0034
glucose 1-phosphate
S108D mutant
0.008
glucose 1-phosphate
H109Q mutant
0.008
glucose 1-phosphate
K118L mutant
0.009
glucose 1-phosphate
R247A mutant
0.01
glucose 1-phosphate
H308N mutant
0.01
glucose 1-phosphate
S108V mutant
0.012
glucose 1-phosphate
-
0.016
glucose 1-phosphate
H329N mutant
0.0127
alpha-D-glucose 1-phosphate
-
mutant RN110A
0.0132
alpha-D-glucose 1-phosphate
-
mutant R15A
0.0195
alpha-D-glucose 1-phosphate
-
mutant R247A
0.0273
alpha-D-glucose 1-phosphate
-
wild-type
0.0279
alpha-D-glucose 1-phosphate
-
mutant R421C
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0.012 - 7.83
alpha-D-glucose 1-phosphate
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
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crystal structure of the selenomethionine-substituted PMM/PGM at 2.2 A resolution, crystal structure of S108A mutant at 1.75 A resolution
mutant enzyme P368G, hanging drop vapour diffusion method
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
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in complex with inhibitor xylose 1-phosphate or slow substrate ribose 1-phosphate. Both ligands induce an interdomain rearrangement, using different enzyme-ligand interactions
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phospho- and dephospho-enzyme in complex with reaction intermediate glucose 1,6-bisphosphate at 1.9 and 2.0 A
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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
-
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E325A
mutant shows 0.08% of wild type activity
H109Q
6% of wild-type activity
H308N
100% of wild-type activity
H308N/H329N
5% of wild-type activity
H329N
6% of wild-type activity
K118L
4% of wild-type activity
K118L/H109Q
5% of wild-type activity
P368A
mutant shows 10% of wild type activity
P368G
mutant shows 8.7% of wild type activity
R20A
12% of wild-type activity
R247A
9% of wild-type activity
R262A
mutant shows 6.1% of wild type activity
R262A/P368G
mutant shows 2.5% of wild type activity
S108
crystal structure, 5% of wild-type activity
S108A
12% of wild-type activity
S108A/H109Q
6% of wild-type activity
S108A/H308N
3% of wild-type activity
S108D
7% of wild-type activity
S108V
1% of wild-type activity
S10V
5% of wild-type activity
S369A
mutant shows 20.5% of wild type activity
Y17A
mutant shows 0.35% of wild type activity
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
R20A
-
no catalytic activity
R241C
-
0.3% of wild-type acivity, with Km value similar to 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
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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
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
Xu, J.; Sarma, A.V.S.; Wei, Y.; Beamer, L.J.; Van Doren, S.R.
Multiple ligand-bound states of a phosphohexomutase revealed by principal component analysis of NMR peak shifts
Sci. Rep.
7
5343
2017
Pseudomonas aeruginosa (P26276)
brenda