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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
undecaprenol kinase, c55-isoprenoid alcohol phosphokinase, polyisoprenol kinase, undecaprenyl phosphokinase, uoh kinase,
more
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C55-isoprenoid alcohol kinase
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C55-isoprenoid alcohol phosphokinase
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-
-
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C55-isoprenyl alcohol phosphokinase
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-
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isoprenoid alcohol kinase
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-
-
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isoprenoid alcohol phosphokinase
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-
-
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isoprenoid-alcohol kinase
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-
-
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kinase (phosphorylating), isoprenoid alcohol
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-
-
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kinase, isoprenoid alcohol (phosphorylating)
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-
-
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polyisoprenol kinase
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-
-
-
undecaprenyl phosphokinase
-
-
DGKA
-
UDPK
-
-
UOH kinase
-
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ATP + undecaprenol = ADP + undecaprenyl phosphate
-
-
-
-
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phospho group transfer
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-
-
-
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ATP:undecaprenol phosphotransferase
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ATP + (E,E,E)-geranylgeraniol
ADP + (E,E,E)-geranylgeraniyl phosphate
ATP + (Z,E,E)-geranylgeraniol
ADP + (Z,E,E)-geranylgeraniyl phosphate
-
5% of the activity with undecaprenol
-
-
?
ATP + C55-isoprenoid alcohol
ADP + C55-isoprenoid alcohol monophosphate
-
-
-
-
?
ATP + decaprenol
ADP + decaprenyl phosphate
-
-
-
-
?
ATP + dolichol
ADP + dolichyl phosphate
ATP + eicosanol
ADP + eicosanyl phosphate
-
-
-
-
?
ATP + ficaprenol
ADP + ficaprenyl phosphate
ATP + heptaprenol
ADP + heptaprenyl phosphate
-
-
-
-
?
ATP + hexadecanol
ADP + hexadecanyl phosphate
-
-
-
-
?
ATP + octaprenol
ADP + octaprenyl phosphate
-
-
-
-
?
ATP + phytol
ADP + phytyl phosphate
-
-
-
-
?
ATP + solanesol
ADP + solanesyl phosphate
ATP + undecanol
ADP + undecanyl phosphate
-
-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl monophosphate
ATP + undecaprenol
ADP + undecaprenyl phosphate
additional information
?
-
ATP + (E,E,E)-geranylgeraniol
ADP + (E,E,E)-geranylgeraniyl phosphate
-
28% of the activity with ATP
-
-
?
ATP + (E,E,E)-geranylgeraniol
ADP + (E,E,E)-geranylgeraniyl phosphate
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5%, of the activity with ATP
-
-
?
ATP + dolichol
ADP + dolichyl phosphate
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13% of the activity with undecaprenol
-
-
?
ATP + dolichol
ADP + dolichyl phosphate
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26% of the activity with undecaprenol
-
-
?
ATP + dolichol
ADP + dolichyl phosphate
-
-
-
-
?
ATP + dolichol
ADP + dolichyl phosphate
55% turnover
-
-
?
ATP + ficaprenol
ADP + ficaprenyl phosphate
-
-
-
?
ATP + ficaprenol
ADP + ficaprenyl phosphate
-
-
-
-
?
ATP + solanesol
ADP + solanesyl phosphate
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about 85% of the activity with undecaprenol
-
-
?
ATP + solanesol
ADP + solanesyl phosphate
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no activity
-
-
?
ATP + solanesol
ADP + solanesyl phosphate
-
poor substrate
-
-
?
ATP + solanesol
ADP + solanesyl phosphate
-
-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl monophosphate
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best substrate
-
?
ATP + undecaprenol
ADP + undecaprenyl monophosphate
-
best substrate
-
-
?
ATP + undecaprenol
ADP + undecaprenyl monophosphate
56% turnover
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
enzyme is involved in biofilm and smegma formation. Absence of Upk influences colony morphology and bacitracin resistance
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
-
-
?
additional information
?
-
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the diacylglycerol kinase of Escherichia coli shows very low undecaprenol kinase, a true undecaprenol kinase is not found in Escherichia coli
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-
?
additional information
?
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product of the reaction is a substrate for the synthesis of lipid intermediates in peptidoglycan synthesis
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-
?
additional information
?
-
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the product of the reaction, C55-isoprenoid alcohol monophosphate functions in the biosynthesis of bacterial peptidoglycan and lipopolysaccharides
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-
?
additional information
?
-
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the enzyme predominantly affects growth of the cells under stress conditions
-
-
?
additional information
?
-
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the enzyme is also a Mg-ADP-dependent undecaprenyl phosphate phosphatase catalyzing the hydrolysis of C55P to C55OH and a free inorganic phosphate
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ATP + undecaprenol
ADP + undecaprenyl phosphate
additional information
?
-
ATP + undecaprenol
ADP + undecaprenyl phosphate
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-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
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enzyme is involved in biofilm and smegma formation. Absence of Upk influences colony morphology and bacitracin resistance
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
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-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
-
-
-
?
ATP + undecaprenol
ADP + undecaprenyl phosphate
-
-
-
?
additional information
?
-
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the diacylglycerol kinase of Escherichia coli shows very low undecaprenol kinase, a true undecaprenol kinase is not found in Escherichia coli
-
-
?
additional information
?
-
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product of the reaction is a substrate for the synthesis of lipid intermediates in peptidoglycan synthesis
-
-
?
additional information
?
-
-
the product of the reaction, C55-isoprenoid alcohol monophosphate functions in the biosynthesis of bacterial peptidoglycan and lipopolysaccharides
-
-
?
additional information
?
-
-
the enzyme predominantly affects growth of the cells under stress conditions
-
-
?
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ATP
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-
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NaCl
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0.5 M, stimulates about 2-fold
Co2+
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can partially replace Mg2+ in activation, 25% of the activation with Mg2+, optimal concentration is 10 mM
Mg2+
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required
Mg2+
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required, optimal activation at 10 mM
Mg2+
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optimum concentration: 0.01 M
Mg2+
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optimum concentration: 0.01 M
Mg2+
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divalent cation required, Mg2+ most effective, optimal concentration: 0.01 M
Mn2+
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can partially replace Mg2+ in activation
Mn2+
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50% of the activation with Mg2+, optimal concentration is 2.5 mM
Mn2+
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can partially replace Mg2+ in activation
Mn2+
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one-fourth of the activity of Mg2+ at 0.001 M
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Mn2+
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complete inhibition at 0.01 M
Urea
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8 M, 20% inhibition
guanidine hydrochloride
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-
guanidine hydrochloride
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strong inhibition above 100 mM
NaCl
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above 10 mM
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Detergents
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overview: activation by detergents, only neutral detergents with short chain and unsaturated chain hydrophobes are successful activators at 25°C
ditetradecanoylphosphatidylcholine
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good activator
lysophosphatidylglycerol
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good activator
Phospholipid cofactor
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requirements for endogenous and exogenous phospholipids. Enzyme requires a fluid lipid surface for activity, lysophosphatidylglycerol and ditetradecanoylphosphatidylcholine are the best activators
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Phospholipid cofactor
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Phospholipid cofactor
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absolute requirement for a phospholipid cofactor, mixture of phosphatidylglycerol and cardiolipin, either of which is effective alone in restoring the activity of the enzyme
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Phospholipid cofactor
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lipid requirement of the enzyme is nonelectrostatic in nature
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Phospholipid cofactor
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absolute requirement for phospholipid and for detergent
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Phospholipid cofactor
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phospholipid cofactor required
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Phospholipid cofactor
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overview: activation by commercial phospholipids and glycolipids, lipids providing a hydrated, loosely packed, highly fluid environment are often effective activators
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Phospholipid cofactor
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reactivation of apoprotein by synthetic lecithins
-
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0.5
ficaprenol
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pH 8.2, 37°C
0.008 - 0.118
undecaprenol
0.057
ATP
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-
0.057
ATP
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pH 8.5, 25°C, reaction with C55-isoprenoid alcohols from Streptococcus faecalis or ficaprenol
0.218
ATP
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at pH 8.0 and 37°C
0.4
ATP
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pH 8.2, 37°C, reaction with ficaprenol
2
ATP
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pH 8.0, 33°C, reaction with undecaprenol
0.0055
dolichol
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-
0.014
dolichol
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pH 8.0, 33°C
0.008
undecaprenol
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-
0.014
undecaprenol
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pH 8.0, 33°C
0.118
undecaprenol
-
at pH 8.0 and 37°C
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3.4
ATP
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at pH 8.0 and 37°C
4
undecaprenol
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at pH 8.0 and 37°C
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1.3
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with eicosanol as substrate, pH and temperature not specified in the publication
1.9
-
with hexadecanol as substrate, pH and temperature not specified in the publication
2.1
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with undecanol as substrate, pH and temperature not specified in the publication
4.5
-
with dolichol as substrate, pH and temperature not specified in the publication
4.9
-
with solanesol as substrate, pH and temperature not specified in the publication
5.1
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with undecaprenol as substrate, pH and temperature not specified in the publication
5.6
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with phytol as substrate, pH and temperature not specified in the publication
8.8
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with heptaprenol as substrate, pH and temperature not specified in the publication
3.8
-
with decaprenol as substrate, pH and temperature not specified in the publication
3.8
-
with octaprenol as substrate, pH and temperature not specified in the publication
additional information
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-
additional information
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-
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7.2 - 8.8
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pH 7.2: about 80% of maximal activity, pH 8.8: about 70% of maximal activity
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UniProt
brenda
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brenda
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brenda
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brenda
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brenda
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UniProt
brenda
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brenda
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UniProt
brenda
ATCC 8014
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brenda
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brenda
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UniProt
brenda
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brenda
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UniProt
brenda
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brenda
bifunctional diacylglycerol kinase/undecaprenol kinase
UniProt
brenda
mutant strain Tn-1
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-
brenda
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-
brenda
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brenda
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bound to
brenda
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brenda
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exclusively found in the cell membrane fraction
brenda
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located in the plasma membrane with the active site facing the cytosol
brenda
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located in the plasma membrane with the active site facing the cytosol
brenda
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located in the plasma membrane with the active site facing the cytosol
brenda
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evolution
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prokaryotic diacylglycerol kinase and undecaprenol kinase are the lone members of the prokaryotic diacylglycerol kinase and undecaprenol kinase family of multispan membrane enzymes that are very small, lack relationships to any other family of proteins, including water soluble kinases, and that exhibit an unusual structure and active site architecture. The enzymes show complex structure, forming domain-swapped homotrimers in which each monomer subunit has three transmembrane segments. Members of this family are unrelated to the eukaryotic diacylglycerol kinases and their prokaryotic homologs, encoded by the dgkB gene
metabolism
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UDPK activity does not participate in the de novo biosynthetic pathway to undecaprenyl phosphate which does not include free undecaprenol as an intermediate
physiological function
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Gram-negative Escherichia coli does not contain high llevels of free undecaprenol, thus has no need for a undecaprenol kinase
physiological function
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UDPK is essential for sporulation of Bacillus subtilis
physiological function
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UDPK seems to play an analogous role in Gram-positive bacteria, where its importance is evident by the fact that UDPK is essential for biofilm formation by the oral pathogen Streptococcus mutans. Undecaprenol has an unusual function as covalent transmembrane carriers of hydrophilic molecules from the inner to the outer leaflet of the plasma membrane for use in biosynthesis of molecules located in the cell wall or periplasm. UDPK is an important enzyme in Streptococcus mutans required for growth at low pH, for biosynthesis of certain lantibiotics, and for biofilm formation.. It is also a virulence factor for the formation of smooth surface dental caries
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17000
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apoprotein, gel filtration
17000
-
1 * 17000, SDS-PAGE
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monomer
-
1 * 17000, SDS-PAGE
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lipoprotein
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requirements for endogenous and exogenous phospholipids. Enzyme requires a fluid lipid surface for activity, lysophosphatidylglycerol and ditetradecanoylphosphatidylcholine are the best activators
lipoprotein
-
absolute requirement for a phospholipid cofactor, mixture of phosphatidylglycerol and cardiolipin, either of which is effective alone in restoring the activity of the enzyme
lipoprotein
-
lipid requirement of the enzyme is nonelectrostatic in nature
lipoprotein
-
absolute requirement for phospholipid and for detergent
lipoprotein
-
overview: activation by commercial phospholipids and glycolipids, lipids providing a hydrated, loosely packed, highly fluid environment are often effective activators
lipoprotein
-
reactivation of apoprotein by synthetic lecithins
lipoprotein
-
phospholipid cofactor required
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A109S
-
the mutant shows about 85% of wild type activity
D106A
-
the activity of the mutant is less than 5% of the activity of wild type enzyme
D7A
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the mutant shows about 70% of wild type activity
D90A
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the activity of the mutant is less than 10% of the activity of wild type enzyme
D94A
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the mutant shows about 65% of wild type activity
E38A
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the mutant shows about 35% of wild type activity
E79A
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the mutant shows about 1% of wild type activity
E86A
-
the mutant shows about 1% of wild type activity
H44A
-
the mutant shows about 58% of wild type activity
H44E
-
the mutant shows about 1% of wild type activity
H96A
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the mutant shows wild type activity
K102A
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the mutant shows about 80% of wild type activity
K105A
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the mutant shows about 20% of wild type activity
N40A
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the mutant shows about 75% of wild type activity
N82A
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the mutant shows about 1% of wild type activity
N87A
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the mutant shows about 85% of wild type activity
R39A
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the mutant shows about 85% of wild type activity
S11A
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the mutant shows about 95% of wild type activity
S22A
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the mutant shows about 105% of wild type activity
S23A
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the mutant shows wild type activity
S83A
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the mutant shows about 105% of wild type activity
T19A
-
the mutant shows about 95% of wild type activity
T21A
-
the mutant shows about 95% of wild type activity
T29A
-
the mutant shows about 110% of wild type activity
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100
-
pH 8.2, aqueous suspension in Tris-HCl, presence of substrate, t1/2: 10 min
100
-
solution in 1-butanol, activation of nearly 50% after 20 min
100
-
30 min, about 30% loss of activity
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enzyme is quite stable to SDS, recovered from SDS gel slices after solubilization in 1% SDS, 1% 2-mercaptoethanol
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relatively unstable in suspension in water
-
remarkably stable towards SDS, 8 M urea and SH-reagents
-
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1-butanol
-
highly stable
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partial
-
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expression in Escherichia coli
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drug development
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the enzyme is a possible anti-cariogenic drug target
synthesis
one-pot reaction leading to undecaprenyl diphosphate disaccharide and starting from undecaprenol, ATP, and the UDP-sugars using the kinase, PglC and PglA
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Higashi, Y.; Siewert, G.; Strominger, J.L.
Biosynthesis of the peptidoglycan of bacterial cell walls. XIX. Isoprenoid alcohol phosphokinase
J. Biol. Chem.
245
3683-3690
1970
Staphylococcus aureus
brenda
Higashi, Y.; Strominger, J.L.
Biosynthesis of the peptidoglycan of bacterial cell walls. XX. Identification of phosphatidylglycerol and cardiolipin as cofactors for isoprenoid alcohol phosphokinase
J. Biol. Chem.
245
3691-3696
1970
Staphylococcus aureus
brenda
Sandermann, H.; Strominger, J.L.
C55-isoprenoid alcohol phosphokinase: an enzyme soluble in organic solvents
Methods Enzymol.
32
439-446
1974
Staphylococcus aureus
brenda
Kalin, J.R.; Allen, C.M.
Characterization of undecaprenol kinase from Lactobacillus plantarum
Biochim. Biophys. Acta
574
112-122
1979
Lactiplantibacillus plantarum
brenda
Kalin, J.R.; Allen, C.M.
Lipid activation of undecaprenol kinase from Lactobacillus plantarum
Biochim. Biophys. Acta
619
76-89
1980
Lactiplantibacillus plantarum
brenda
Poxton, I.R.; Lomax, J.A.; Sutherland, I.W.
Isoprenoid alcohol kinase--a third butanol-soluble enzyme in Klebsiella aerogenes membranes
J. Gen. Microbiol.
84
231-233
1974
Klebsiella aerogenes
brenda
Sandermann, H.
Reactivation of C55-isoprenoid alcohol phosphokinase apoprotein by synthetic lecithins
FEBS Lett.
21
254-258
1972
Staphylococcus aureus
brenda
Sandermann, H.; Strominger, J.L.
C 55 -isoprenoid alcohol phosphokinase: an extremely hydrophobic protein from the bacterial membrane
Proc. Natl. Acad. Sci. USA
68
2441-2443
1971
Staphylococcus aureus
brenda
Gennis, R.B.; Strominger, J.L.
Activation of C55-isoprenoid alcohol phosphokinase from Staphylococcus aureus. I. Activation by phospholipids and fatty acids
J. Biol. Chem.
251
1264-1269
1976
Staphylococcus aureus
brenda
Gennis, R.B.; Strominger, J.L.
Activation of C55-isoprenoid alcohol phosphokinase from Staphylococcus aureus. III. Activation by detergents
J. Biol. Chem.
251
1277-1282
1976
Staphylococcus aureus
brenda
Sandermann, H.; Strominger, J.L.
Purification and properties of C 55 -isoprenoid alcohol phosphokinase from Staphylococcus aureus
J. Biol. Chem.
247
5123-5131
1972
Staphylococcus aureus
brenda
Lis, M.; Kuramitsu, H.K.
The stress-responsive dgk gene from Streptococcus mutans encodes a putative undecaprenol kinase activity
Infect. Immun.
71
1938-1943
2003
Streptococcus mutans
brenda
Rose, L.; Kaufmann, S.H.; Daugelat, S.
Involvement of Mycobacterium smegmatis undecaprenyl phosphokinase in biofilm and smegma formation
Microbes Infect.
6
965-971
2004
Mycolicibacterium smegmatis
brenda
Hartley, M.D.; Larkin, A.; Imperiali, B.
Chemoenzymatic synthesis of polyprenyl phosphates
Bioorg. Med. Chem.
16
5149-5156
2008
Streptococcus mutans (Q05888)
brenda
Van Horn, W.D.; Sanders, C.R.
Prokaryotic diacylglycerol kinase and undecaprenol kinase
Annu. Rev. Biophys.
41
81-101
2012
Bacillus subtilis, Escherichia coli, Streptococcus mutans
brenda
Huang, L.Y.; Huang, S.H.; Chang, Y.C.; Cheng, W.C.; Cheng, T.J.; Wong, C.H.
Enzymatic synthesis of lipid II and analogues
Angew. Chem. Int. Ed. Engl.
53
8060-8065
2014
Streptococcus mutans
brenda
Kawakami, N.; Fujisaki, S.
Undecaprenyl phosphate metabolism in Gram-negative and Gram-positive bacteria
Biosci. Biotechnol. Biochem.
82
940-946
2018
Staphylococcus aureus (A0A0D1H2F6), Staphylococcus aureus, Lactiplantibacillus plantarum (A0A151G991), Bacillus subtilis (P19638), Streptococcus mutans (Q05888), Bacillus subtilis 168 (P19638)
brenda
Huang, L.Y.; Wang, S.C.; Cheng, T.R.; Wong, C.H.
Undecaprenyl Phosphate Phosphatase Activity of Undecaprenol Kinase Regulates the Lipid Pool in Gram-Positive Bacteria
Biochemistry
56
5417-5427
2017
Streptococcus mutans
brenda
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