BRENDA - Enzyme Database
show all sequences of 2.7.1.197

Substrate and phospholipid specificity of the purified mannitol permease of Escherichia coli

Jacobson, G.; Tanney, L.; Kelly, D.; Palman, K.; Corn, S.; J. Cell. Biochem. 23, 231-240 (1983)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
cardiolipin
-
Escherichia coli
phosphatidylethanolamine
-
Escherichia coli
phosphatidylglycerol
-
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-amino-2-deoxy-D-mannitol
63% residual activity at 2 mM
Escherichia coli
2-deoxy-D-mannitol
73% residual activity at 2 mM; 74% residual activity at 2 mM
Escherichia coli
D-arabitol
-
Escherichia coli
D-glucitol
73% residual activity at 2 mM
Escherichia coli
D-mannoheptitol
9% residual activity at 2 mM
Escherichia coli
D-mannonic acid
-
Escherichia coli
additional information
1,6-dibromo-1,6-dideoxy-D-mannitol, D,L-threitol, L-threitol, erythritol, and glycerol do not inhibit the enzyme
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
D-mannitol[side 1]
at pH 8.0 and 37°C
Escherichia coli
0.2
-
2-amino-2-deoxy-D-mannitol[side 1]
at pH 8.0 and 37°C
Escherichia coli
0.5
-
2-deoxy-D-mannitol[side 1]
at pH 8.0 and 37°C
Escherichia coli
0.5
-
D-arabitol[side 1]
Km above 0.5 mM, at pH 8.0 and 37°C
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
Escherichia coli
the enzyme is highly, but not absolutely, specific for D-mannitol
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P00550
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
no activity with D-galactitol, D-ribitol, and D-xylitol
736548
Escherichia coli
?
-
-
-
-
[protein]-Npi-phospho-L-histidine + 2-amino-2-deoxy-D-mannitol[side 1]
50% activity compared to D-mannitol
736548
Escherichia coli
[protein]-L-histidine + 2-amino-2-deoxy-D-mannitol 1-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + 2-deoxy-D-mannitol[side 1]
32% activity compared to D-mannitol
736548
Escherichia coli
[protein]-L-histidine + 2-deoxy-D-mannitol 1-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-arabitol[side 1]
11% activity compared to D-mannitol
736548
Escherichia coli
[protein]-L-histidine + D-arabitol 1-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucitol[side 1]
37% activity compared to D-mannitol
736548
Escherichia coli
[protein]-L-histidine + D-glucitol 1-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
the enzyme is highly, but not absolutely, specific for D-mannitol
736548
Escherichia coli
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Escherichia coli
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
cardiolipin
-
Escherichia coli
phosphatidylethanolamine
-
Escherichia coli
phosphatidylglycerol
-
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-amino-2-deoxy-D-mannitol
63% residual activity at 2 mM
Escherichia coli
2-deoxy-D-mannitol
73% residual activity at 2 mM; 74% residual activity at 2 mM
Escherichia coli
D-arabitol
-
Escherichia coli
D-glucitol
73% residual activity at 2 mM
Escherichia coli
D-mannoheptitol
9% residual activity at 2 mM
Escherichia coli
D-mannonic acid
-
Escherichia coli
additional information
1,6-dibromo-1,6-dideoxy-D-mannitol, D,L-threitol, L-threitol, erythritol, and glycerol do not inhibit the enzyme
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
D-mannitol[side 1]
at pH 8.0 and 37°C
Escherichia coli
0.2
-
2-amino-2-deoxy-D-mannitol[side 1]
at pH 8.0 and 37°C
Escherichia coli
0.5
-
2-deoxy-D-mannitol[side 1]
at pH 8.0 and 37°C
Escherichia coli
0.5
-
D-arabitol[side 1]
Km above 0.5 mM, at pH 8.0 and 37°C
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
Escherichia coli
the enzyme is highly, but not absolutely, specific for D-mannitol
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
no activity with D-galactitol, D-ribitol, and D-xylitol
736548
Escherichia coli
?
-
-
-
-
[protein]-Npi-phospho-L-histidine + 2-amino-2-deoxy-D-mannitol[side 1]
50% activity compared to D-mannitol
736548
Escherichia coli
[protein]-L-histidine + 2-amino-2-deoxy-D-mannitol 1-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + 2-deoxy-D-mannitol[side 1]
32% activity compared to D-mannitol
736548
Escherichia coli
[protein]-L-histidine + 2-deoxy-D-mannitol 1-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-arabitol[side 1]
11% activity compared to D-mannitol
736548
Escherichia coli
[protein]-L-histidine + D-arabitol 1-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucitol[side 1]
37% activity compared to D-mannitol
736548
Escherichia coli
[protein]-L-histidine + D-glucitol 1-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannitol[side 1]
the enzyme is highly, but not absolutely, specific for D-mannitol
736548
Escherichia coli
[protein]-L-histidine + D-mannitol 1-phosphate[side 2]
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Escherichia coli
Other publictions for EC 2.7.1.197
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
736402
Veldhuis
Substrate-induced conformation ...
Escherichia coli
J. Biol. Chem.
280
35148-35156
2005
-
-
-
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1
-
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1
-
2
-
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1
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1
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1
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1
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1
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1
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641879
Van Montfort
The structure of the Escherich ...
Escherichia coli
Structure
6
377-388
1998
-
-
1
1
-
-
-
-
1
-
1
1
-
3
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
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-
1
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1
-
-
-
-
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1
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1
1
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1
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1
1
-
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-
-
-
-
-
-
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-
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-
735662
Meijberg
Interdomain interactions betwe ...
Escherichia coli
Biochemistry
35
2759-2766
1996
-
-
-
-
-
-
-
-
1
-
-
1
-
2
-
-
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1
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1
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1
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-
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
735658
Lolkema
Mannitol-specific enzyme II of ...
Escherichia coli, Escherichia coli ML308-225
Biochemistry
32
1396-1400
1993
-
-
-
-
-
-
-
-
1
-
3
2
-
5
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
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1
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3
2
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1
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-
-
2
1
-
-
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-
-
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-
-
-
-
-
-
-
-
736381
Jacobson
The Escherichia coli mannitol ...
Escherichia coli
J. Bioenerg. Biomembr.
25
621-626
1993
-
-
-
-
5
-
-
-
1
-
-
1
-
2
-
-
-
-
-
-
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-
1
-
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-
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5
-
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1
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1
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-
1
-
-
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-
-
735657
Van Dijk
Characterization of the proton ...
Escherichia coli, Escherichia coli JC411
Biochemistry
31
9063-9072
1992
-
-
-
-
-
-
-
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2
-
2
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1
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2
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2
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1
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2
-
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736389
Weng
Site-specific mutagenesis of r ...
Escherichia coli
J. Biol. Chem.
267
19529-19535
1992
-
-
1
-
8
-
-
-
2
-
1
1
-
2
-
-
-
-
-
-
-
-
1
-
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1
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8
-
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2
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1
1
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-
1
-
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737220
Jacobson
Interrelationships between pro ...
Escherichia coli
Res. Microbiol.
143
113-116
1992
-
-
-
-
2
-
-
-
1
-
-
1
-
2
-
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1
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2
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1
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1
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1
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735656
Lolkema
Subunit structure and activity ...
Escherichia coli, Escherichia coli ML308-225
Biochemistry
29
10120-10125
1990
-
-
-
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-
2
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1
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2
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5
-
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2
1
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2
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1
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2
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2
1
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736333
Elferink
Functional reconstitution of t ...
Escherichia coli
J. Bacteriol.
172
7119-7125
1990
-
-
-
-
-
-
2
2
1
-
1
1
-
2
-
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1
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1
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2
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2
1
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1
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1
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1
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736126
Jacobson
Structural and functional doma ...
Escherichia coli
FEMS Microbiol. Rev.
63
25-34
1989
-
-
1
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2
-
1
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3
1
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2
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1
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2
1
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1
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1
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1
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1
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2
1
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736549
Khandekar
Evidence for two distinct conf ...
Escherichia coli, Escherichia coli KL141
J. Cell. Biochem.
39
207-216
1989
1
-
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4
1
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3
2
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3
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1
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2
1
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1
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1
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735654
Pas
S-phosphocysteine and phosphoh ...
Escherichia coli
Biochemistry
27
5835-5839
1988
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1
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735655
Reiche
Staphylococcal phosphoenolpyru ...
Escherichia coli
Biochemistry
27
6512-6516
1988
-
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1
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4
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736794
Robillard
The redox state and the phosph ...
Escherichia coli
Mol. Cell. Biochem.
82
113-118
1988
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1
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1
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641863
Sutrina
HPr/HPr-P phosphoryl exchange ...
Escherichia coli
J. Biol. Chem.
262
2636-2641
1987
-
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-
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3
-
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1
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2
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3
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1
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1
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1
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641866
Jacobson
Mannitol-specific enzyme II of ...
Escherichia coli
J. Biol. Chem.
258
10748-10756
1983
1
-
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7
1
2
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1
2
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2
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1
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3
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1
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7
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2
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2
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3
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1
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641867
Leonard
Mannitol-specific enzyme II of ...
Escherichia coli
J. Biol. Chem.
258
10757-10760
1983
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1
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736548
Jacobson
Substrate and phospholipid spe ...
Escherichia coli
J. Cell. Biochem.
23
231-240
1983
3
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7
4
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2
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6
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7
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6
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1
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1
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641875
Jacobson
Purification of the mannitol-s ...
Escherichia coli
J. Biol. Chem.
254
249-252
1979
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