BRENDA - Enzyme Database
show all sequences of 2.4.99.B6

Enzymatic synthesis of lipopolysaccharide in Escherichia coli. Purification and properties of heptosyltransferase I

Kadrmas, J.L.; Raetz, C.R.; J. Biol. Chem. 273, 2799-2807 (1998)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
Triton X-100
the enzymatic activity is dependent upon the presence of Triton X-100. At concentrations greater than 0.1% Triton X-100, the transferase activity is inhibited
Escherichia coli
Cloned(Commentary)
Cloned (Commentary)
Organism
-
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
Triton X-100
the enzymatic activity is dependent upon the presence of Triton X-100. At concentrations greater than 0.1% Triton X-100, the transferase activity is inhibited
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0045
-
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH 7.5, 30C
Escherichia coli
1.5
-
ADP-alpha-D-mannose
pH 7.5, 30C
Escherichia coli
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Escherichia coli
16020
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
x * 36000, gel electrophoresis
Escherichia coli
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Escherichia coli
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
4.9
-
pH 7.5, 30C
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
ADP-alpha-D-mannose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
i.e. alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA. In cell extracts, ADP-mannose can serve as an alternative donor, but is mannosylated at less than 1% the rate of alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA
727824
Escherichia coli
ADP + ?
-
-
-
?
ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
i.e. alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA. It is possible to assay the enzyme in crude cell extracts using ADP-mannose in place of ADP-L-glycero-beta-D-manno-heptose. No activity without detergent
727824
Escherichia coli
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
-
-
-
?
additional information
the purified enzyme displays no activity with ADP-glucose, GDP-mannose, UDP-glucose, or UDP-galactose
727824
Escherichia coli
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 36000, gel electrophoresis
Escherichia coli
Synonyms
Synonyms
Commentary
Organism
heptosyltransferase I
-
Escherichia coli
rfaC
-
Escherichia coli
waaC
-
Escherichia coli
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Escherichia coli
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7.2
8
pH 7.2: about 70% of maximal activity, pH 8.0: about 55% of maximal activity
Escherichia coli
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Triton X-100
the enzymatic activity is dependent upon the presence of Triton X-100. At concentrations greater than 0.1% Triton X-100, the transferase activity is inhibited
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Triton X-100
the enzymatic activity is dependent upon the presence of Triton X-100. At concentrations greater than 0.1% Triton X-100, the transferase activity is inhibited
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0045
-
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH 7.5, 30C
Escherichia coli
1.5
-
ADP-alpha-D-mannose
pH 7.5, 30C
Escherichia coli
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Escherichia coli
16020
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
x * 36000, gel electrophoresis
Escherichia coli
Purification (Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
4.9
-
pH 7.5, 30C
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
ADP-alpha-D-mannose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
i.e. alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA. In cell extracts, ADP-mannose can serve as an alternative donor, but is mannosylated at less than 1% the rate of alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA
727824
Escherichia coli
ADP + ?
-
-
-
?
ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
i.e. alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA. It is possible to assay the enzyme in crude cell extracts using ADP-mannose in place of ADP-L-glycero-beta-D-manno-heptose. No activity without detergent
727824
Escherichia coli
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
-
-
-
?
additional information
the purified enzyme displays no activity with ADP-glucose, GDP-mannose, UDP-glucose, or UDP-galactose
727824
Escherichia coli
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 36000, gel electrophoresis
Escherichia coli
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Escherichia coli
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7.2
8
pH 7.2: about 70% of maximal activity, pH 8.0: about 55% of maximal activity
Escherichia coli
General Information
General Information
Commentary
Organism
malfunction
lipopolysaccharide isolated from mutants defective in rfaC lack heptose and all other sugars distal to heptose
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
malfunction
lipopolysaccharide isolated from mutants defective in rfaC lack heptose and all other sugars distal to heptose
Escherichia coli
Other publictions for EC 2.4.99.B6
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
Synonyms
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)
737682
Czyzyk
Escherichia coli heptosyltrans ...
Escherichia coli
Biochemistry
52
5158-5160
2013
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726955
Czyzyk
Lipopolysaccharide biosynthesi ...
Escherichia coli
Biochemistry
50
10570-10572
2011
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8
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1
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2
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6
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1
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8
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8
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6
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8
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1
1
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8
8
727326
Durka
The inhibition of liposacchari ...
Escherichia coli
Chemistry
18
641-651
2011
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1
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1
1
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727135
Moreau
Discovery of new Gram-negative ...
Escherichia coli
Bioorg. Med. Chem. Lett.
18
4022-4026
2008
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1
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-
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11
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-
1
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1
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1
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10
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1
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11
10
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1
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728139
Grizot
Structure of the Escherichia c ...
Escherichia coli
J. Mol. Biol.
363
383-394
2006
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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
1
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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1
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1
1
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728049
Gronow
Characterization of the physio ...
Escherichia coli
J. Endotoxin Res.
7
263-270
2001
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1
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3
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2
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727413
Gronow
Comparative functional charact ...
Escherichia coli
Eur. J. Biochem.
267
6602-6611
2000
-
-
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3
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1
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1
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2
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1
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1
1
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727824
Kadrmas
Enzymatic synthesis of lipopol ...
Escherichia coli
J. Biol. Chem.
273
2799-2807
1998
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