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show all sequences of 2.7.1.130

Crystal structure of LpxK, the 4-kinase of lipid A biosynthesis and atypical P-loop kinase functioning at the membrane interface

Emptage, R.P.; Daughtry, K.D.; Pemble, C.W.; Raetz, C.R.; Proc. Natl. Acad. Sci. USA 109, 12956-12961 (2012)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
apo- and ADP/Mg2+-bound forms, to a resolution of 1.9 A and 2.2 A, respectively. The enzyme consists of two alpha/beta/alpha sandwich domains connected by a two-stranded beta-sheet linker. The N-terminal domain, which has most structural homology to other family members, is responsible for catalysis at the P-loop and positioning of the disaccharide 1-phosphate substrate for phosphoryl transfer on the inner membrane. The smaller C-terminal domain helps to bind the nucleotide substrate and Mg2+ cation using a 25° hinge motion about its base
Aquifex aeolicus
Engineering
Amino acid exchange
Commentary
Organism
D138A
point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity
Aquifex aeolicus
D139A
point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity
Aquifex aeolicus
G47A
about 43% of wild-type activity
Aquifex aeolicus
G48A
about 1.8% of wild-type activity
Aquifex aeolicus
G50A
about 0.1% of wild-type activity
Aquifex aeolicus
K51A
about 0.1% of wild-type activity
Aquifex aeolicus
S53A
about 9.9% of wild-type activity
Aquifex aeolicus
T52A
about 0.1% of wild-type activity
Aquifex aeolicus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aquifex aeolicus
O67572
-
-
Crystallization (Commentary) (protein specific)
Crystallization
Organism
apo- and ADP/Mg2+-bound forms, to a resolution of 1.9 A and 2.2 A, respectively. The enzyme consists of two alpha/beta/alpha sandwich domains connected by a two-stranded beta-sheet linker. The N-terminal domain, which has most structural homology to other family members, is responsible for catalysis at the P-loop and positioning of the disaccharide 1-phosphate substrate for phosphoryl transfer on the inner membrane. The smaller C-terminal domain helps to bind the nucleotide substrate and Mg2+ cation using a 25° hinge motion about its base
Aquifex aeolicus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D138A
point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity
Aquifex aeolicus
D139A
point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity
Aquifex aeolicus
G47A
about 43% of wild-type activity
Aquifex aeolicus
G48A
about 1.8% of wild-type activity
Aquifex aeolicus
G50A
about 0.1% of wild-type activity
Aquifex aeolicus
K51A
about 0.1% of wild-type activity
Aquifex aeolicus
S53A
about 9.9% of wild-type activity
Aquifex aeolicus
T52A
about 0.1% of wild-type activity
Aquifex aeolicus
Other publictions for EC 2.7.1.130
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)
738621
Emptage
Structural basis of lipid bind ...
Aquifex aeolicus
J. Biol. Chem.
289
24059-24068
2014
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1
1
1
15
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12
1
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1
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1
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15
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15
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12
1
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1
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15
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2
2
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737675
Emptage
Mechanistic characterization o ...
Aquifex aeolicus
Biochemistry
52
2280-2290
2013
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1
1
17
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5
19
1
4
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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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15
3
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1
1
17
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5
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19
1
4
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2
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1
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15
3
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4
4
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723650
Emptage
Crystal structure of LpxK, the ...
Aquifex aeolicus
Proc. Natl. Acad. Sci. USA
109
12956-12961
2012
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1
8
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640807
Garrett
Identification of the gene enc ...
Escherichia coli
J. Biol. Chem.
272
21855-21864
1997
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640806
Hampton
Lipid A 4-kinase from Escheric ...
Escherichia coli
Methods Enzymol.
209
466-475
1992
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640805
Ray
The biosynthesis of gram-negat ...
Escherichia coli
J. Biol. Chem.
262
1122-1128
1987
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