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[heat stable phosphocarrier protein HPr]-Npi-phospho-L-histidine + D-mannitol[side 1]
[heat stable phosphocarrier protein HPr]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
?
[heat-stable phosphocarrier protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[heat-stable phosphocarrier protein]-L-histidine + D-mannitol 1-phosphate[side 2]
[protein HPr]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein HPr]-L-histidine + D-mannitol 1-phosphate[side 2]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
-
-
-
r
[protein]-Npi-phospho-L-histidine + 2-amino-2-deoxy-D-mannitol[side 1]
[protein]-L-histidine + 2-amino-2-deoxy-D-mannitol 1-phosphate[side 2]
50% activity compared to D-mannitol
-
-
?
[protein]-Npi-phospho-L-histidine + 2-deoxy-D-mannitol[side 1]
[protein]-L-histidine + 2-deoxy-D-mannitol 1-phosphate[side 2]
32% activity compared to D-mannitol
-
-
?
[protein]-Npi-phospho-L-histidine + D-arabitol[side 1]
[protein]-L-histidine + D-arabitol 1-phosphate[side 2]
11% activity compared to D-mannitol
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucitol[side 1]
[protein]-L-histidine + D-glucitol 1-phosphate[side 2]
37% activity compared to D-mannitol
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
additional information
?
-
[heat-stable phosphocarrier protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[heat-stable phosphocarrier protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
r
[heat-stable phosphocarrier protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[heat-stable phosphocarrier protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
r
[protein HPr]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein HPr]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
?
[protein HPr]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein HPr]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
?
[protein HPr]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein HPr]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
r
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
ir
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
r
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
r
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
the enzyme is highly, but not absolutely, specific for D-mannitol
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
r
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
ir
additional information
?
-
no activity with D-galactitol, D-ribitol, and D-xylitol
-
-
?
additional information
?
-
-
no activity with D-galactitol, D-ribitol, and D-xylitol
-
-
?
additional information
?
-
-
substrate specificity: mannitol>>2-amino-2-deoxymannitol, 2-deoxymannitol, glucitol >> arabinitol, mannonic acid
-
-
?
additional information
?
-
the purified enzyme does not catalyze hydrolysis of D-mannitol 1-phosphate
-
-
?
additional information
?
-
-
the purified enzyme does not catalyze hydrolysis of D-mannitol 1-phosphate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
[heat stable phosphocarrier protein HPr]-Npi-phospho-L-histidine + D-mannitol[side 1]
[heat stable phosphocarrier protein HPr]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
?
[heat-stable phosphocarrier protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[heat-stable phosphocarrier protein]-L-histidine + D-mannitol 1-phosphate[side 2]
[protein HPr]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein HPr]-L-histidine + D-mannitol 1-phosphate[side 2]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
-
-
-
r
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
[heat-stable phosphocarrier protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[heat-stable phosphocarrier protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
r
[heat-stable phosphocarrier protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[heat-stable phosphocarrier protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
r
[protein HPr]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein HPr]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
?
[protein HPr]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein HPr]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
?
[protein HPr]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein HPr]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
r
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
ir
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
r
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
r
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
the enzyme is highly, but not absolutely, specific for D-mannitol
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
r
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
-
ir
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-amino-2-deoxy-D-mannitol
63% residual activity at 2 mM
2-deoxy-D-mannitol
73% residual activity at 2 mM; 74% residual activity at 2 mM
D-fructose 1,6-bisphosphate
34% inhibition at 20 mM
D-mannitol
strong substrate inhibition at pH 7.0
D-mannitol 1-phosphate
strong substrate inhibition at pH 7.0
D-mannoheptitol
9% residual activity at 2 mM
diethyldicarbonate
-
complete inactivation at 1 mM
Mg2+
-
Mg2+ ions at sufficiently high concentrations (5 mM) inhibit enzyme
phosphate
-
a 5fold dilution of a mixture of 10 mM phosphate, 5 mM MgSO4, and 50 mM NaF into phosphate buffers, pH 6.0-6.3 just before the zero time point leads to a rapid inhibition of the enzyme activity
D-glucitol
-
D-glucitol
73% residual activity at 2 mM
N-ethylmaleimide
-
-
N-ethylmaleimide
rapid inactivation with 0.5 mM
N-ethylmaleimide
-
92% inhibition at 4 mM
N-ethylmaleimide
-
irreversible inhibition
Trypsin
-
-
Trypsin
-
the enzyme is very sensitive to trypsin which cleaves it into 2 fragments (ca. 30 kDa each) with concomitant inactivation
-
Trypsin
-
0.0005 mg/ml trypsin degrades half of the enzyme molecules in intact liposomes
-
additional information
-
not inhibited by EDTA
-
additional information
1,6-dibromo-1,6-dideoxy-D-mannitol, D,L-threitol, L-threitol, erythritol, and glycerol do not inhibit the enzyme
-
additional information
-
1,6-dibromo-1,6-dideoxy-D-mannitol, D,L-threitol, L-threitol, erythritol, and glycerol do not inhibit the enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Sutrina, S.L.; Waygood, E.B.; Grenier, F.C.; Saier, M.H.
HPr/HPr-P phosphoryl exchange reaction catalyzed by the mannitol specific enzyme II of the bacterial phosphotransferase system
J. Biol. Chem.
262
2636-2641
1987
Escherichia coli
brenda
Jacobson, G.R.; Lee, C.A.; Leonard, J.E.; Saier, M.H.
Mannitol-specific enzyme II of the bacterial phosphotransferase system. I. Properties of the purified permease
J. Biol. Chem.
258
10748-10756
1983
Escherichia coli (P00550), Escherichia coli
brenda
Leonard, J.E.; Saier, M.H.
Mannitol-specific enzyme II of the bacterial phosphotransferase system. II. Reconstitution of vectorial transphosphorylation in phospholipid vesicles
J. Biol. Chem.
258
10757-10760
1983
Escherichia coli
brenda
Jacobson, G.R.; Lee, C.A.; Saier, M.H.
Purification of the mannitol-specific enzyme II of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system
J. Biol. Chem.
254
249-252
1979
Escherichia coli (P00550), Escherichia coli
brenda
Van Montfort, R.L.M.; Pijning, T.; Kalk, K.H.; Hangyi, I.; Kouwijzer, M.L.C.E.; Robillard, G.T.; Dijkstra, B.W.
The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site
Structure
6
377-388
1998
Escherichia coli (P00550), Escherichia coli
brenda
Pas, H.H.; Robillard, G.T.
S-phosphocysteine and phosphohistidine are intermediates in the phosphoenolpyruvate-dependent mannitol transport catalyzed by Escherichia coli EIIMtl
Biochemistry
27
5835-5839
1988
Escherichia coli
brenda
Reiche, B.; Frank, R.; Deutscher, J.; Meyer, N.; Hengstenberg, W.
Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system: Purification and characterization of the mannitol-specific enzyme IIImtl of Staphylococcus aureus and Staphylococcus carnosus and homology with the enzyme IImtl of Escherichia coli
Biochemistry
27
6512-6516
1988
Escherichia coli
brenda
Lolkema, J.; Robillard, G.
Subunit structure and activity of the mannitol-specific enzyme II of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system solubilized in detergent
Biochemistry
29
10120-10125
1990
Escherichia coli, Escherichia coli ML308-225
brenda
Van Dijk, A.; Scheek, R.; Dijkstra, K.; Wolters, G.; Robillard, G.
Characterization of the protonation and hydrogen bonding state of the histidine residues in IIA(mtl), a domain of the phosphoenolpyruvate-dependent mannitol-specific transport protein
Biochemistry
31
9063-9072
1992
Escherichia coli, Escherichia coli JC411
brenda
Lolkema, J.S.; Kuiper, H.; ten Hoeve-Duurkens, R.H.; Robillard, G.T.
Mannitol-specific enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli: Physical size of enzyme IImtl and its domains IIBA and IIC in the active state
Biochemistry
32
1396-1400
1993
Escherichia coli, Escherichia coli ML308-225
brenda
Meijberg, W.; Schuurman-Wolters, G.; Robillard, G.
Interdomain interactions between the hydrophilic domains of the mannitol transporter of Escherichia coli in the unphosphorylated and phosphorylated states
Biochemistry
35
2759-2766
1996
Escherichia coli (P00550), Escherichia coli
brenda
Jacobson, G.; Stephan, M.
Structural and functional domains of the mannitol-specific enzyme II of the E. coli phosphoenolpyruvate-dependent phosphotransferase system
FEMS Microbiol. Rev.
63
25-34
1989
Escherichia coli
brenda
Elferink, M.; Driessen, A.; Ribillard, G.
Functional reconstitution of the purified phosphoenolpyruvate-dependent mannitol-specific transport system of Escherichia coli in phospholipid vesicles: Coupling between transport and phosphorylation
J. Bacteriol.
172
7119-7125
1990
Escherichia coli
brenda
Jacobson, G.; Saraceni-Richards, C.
The Escherichia coli mannitol permease as a model for transport via the bacterial phosphotransferase system
J. Bioenerg. Biomembr.
25
621-626
1993
Escherichia coli (P00550), Escherichia coli
brenda
Weng, Q.; Elder, J.; Jacobson, G.
Site-specific mutagenesis of residues in the Escherichia coli mannitol permease that have been suggested to be important for its phosphorylation and chemoreception functions
J. Biol. Chem.
267
19529-19535
1992
Escherichia coli (P00550), Escherichia coli
brenda
Veldhuis, G.; Gabellieri, E.; Vos, E.; Poolman, B.; Strambini, G.; Broos, J.
Substrate-induced conformational changes in the membrane-embedded IIc mtl-domain of the mannitol permease from Escherichia coli, EnzymeIImtl, probed by tryptophan phosphorescence spectroscopy
J. Biol. Chem.
280
35148-35156
2005
Escherichia coli
brenda
Jacobson, G.; Tanney, L.; Kelly, D.; Palman, K.; Corn, S.
Substrate and phospholipid specificity of the purified mannitol permease of Escherichia coli
J. Cell. Biochem.
23
231-240
1983
Escherichia coli (P00550), Escherichia coli
brenda
Khandekar, S.; Jacobson, G.
Evidence for two distinct conformations of the Escherichia coli mannitol permease that are important for its transport and phosphorylation functions
J. Cell. Biochem.
39
207-216
1989
Escherichia coli, Escherichia coli KL141
brenda
Robillard, G.; Pas, H.; Gage, D.; Elferink, M.
The redox state and the phosphorylation state of the mannitol-specific carrier of the E. coli phosphoenolpyruvate-dependent phosphotransferase system
Mol. Cell. Biochem.
82
113-118
1988
Escherichia coli
brenda
Jacobson, G.
Interrelationships between protein phosphorylation and oligomerization in transport and chemotaxis via the Escherichia coli mannitol phosphotransferase system
Res. Microbiol.
143
113-116
1992
Escherichia coli
brenda
Lee, K.; Kim, E.; Kim, G.; Jung, J.; Katayama, S.; Nakamura, S.; Suh, J.
Biophysical characterization of the domain association between cytosolic A and B domains of the mannitol transporter enzymes IIMtl in the presence and absence of a connecting linker
Protein Sci.
25
1803-1811
2016
Caldanaerobacter subterraneus subsp. tengcongensis
brenda