BRENDA - Enzyme Database show
show all sequences of 2.3.1.181

Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase

Nesbitt, N.M.; Baleanu-Gogonea, C.; Cicchillo, R.M.; Goodson, K.; Iwig, D.F.; Broadwater, J.A.; Haas, J.A.; Fox, B.G.; Booker, S.J.; Protein Expr. Purif. 39, 269-282 (2005)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
KHCO3
100 mM, slight activation
Escherichia coli
NaOAc
100 mM, slight activation
Escherichia coli
Cloned(Commentary)
Commentary
Organism
N-terminal hexahistidine-tagged apo-H protein
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
Octanoyl-CoA
0.5 mM, 67% inhibition
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0102
-
octanoyl-[acyl-carrier protein]
pH 7.2, 37°C
Escherichia coli
0.0132
-
apo-H protein
pH 7.2, 37°C
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
10000
-
monomer, gel filtration
Escherichia coli
29000
-
trimer, gel filtration
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
octanoyl-[acyl-carrier protein] + apo-H protein
Escherichia coli
LipB reaction represents the first committed step in the biosynthesis of the lipoyl cofactor. apo-H protein is the lipoyl bearing subunit of the glycine cleavage system
APO H-protein N6-(octanoyl)lysine + acyl-carrier protein
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Purification (Commentary)
Commentary
Organism
N-terminal hexahistidine-tagged apo-H protein
Escherichia coli
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.54
-
-
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
octanoyl-[acyl-carrier protein] + apo-H protein
LipB reaction represents the first committed step in the biosynthesis of the lipoyl cofactor. apo-H protein is the lipoyl bearing subunit of the glycine cleavage system
663308
Escherichia coli
APO H-protein N6-(octanoyl)lysine + acyl-carrier protein
-
-
-
?
octanoyl-[acyl-carrier protein] + apo-H protein
apo-H protein is the lipoyl bearing subunit of the glycine cleavage system
663308
Escherichia coli
apo-H protein N6-(octanoyl)lysine + acyl-carrier protein
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.2
-
apo-H protein
pH 7.2, 37°C
Escherichia coli
0.2
-
octanoyl-[acyl-carrier protein]
pH 7.2, 37°C
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Escherichia coli
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
9
pH 6.0: about 65% of maximal activity, pH 9.0: about 40% of maximal activity
Escherichia coli
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
KHCO3
100 mM, slight activation
Escherichia coli
NaOAc
100 mM, slight activation
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
N-terminal hexahistidine-tagged apo-H protein
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Octanoyl-CoA
0.5 mM, 67% inhibition
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0102
-
octanoyl-[acyl-carrier protein]
pH 7.2, 37°C
Escherichia coli
0.0132
-
apo-H protein
pH 7.2, 37°C
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
10000
-
monomer, gel filtration
Escherichia coli
29000
-
trimer, gel filtration
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
octanoyl-[acyl-carrier protein] + apo-H protein
Escherichia coli
LipB reaction represents the first committed step in the biosynthesis of the lipoyl cofactor. apo-H protein is the lipoyl bearing subunit of the glycine cleavage system
APO H-protein N6-(octanoyl)lysine + acyl-carrier protein
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
N-terminal hexahistidine-tagged apo-H protein
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.54
-
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
octanoyl-[acyl-carrier protein] + apo-H protein
LipB reaction represents the first committed step in the biosynthesis of the lipoyl cofactor. apo-H protein is the lipoyl bearing subunit of the glycine cleavage system
663308
Escherichia coli
APO H-protein N6-(octanoyl)lysine + acyl-carrier protein
-
-
-
?
octanoyl-[acyl-carrier protein] + apo-H protein
apo-H protein is the lipoyl bearing subunit of the glycine cleavage system
663308
Escherichia coli
apo-H protein N6-(octanoyl)lysine + acyl-carrier protein
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.2
-
apo-H protein
pH 7.2, 37°C
Escherichia coli
0.2
-
octanoyl-[acyl-carrier protein]
pH 7.2, 37°C
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
6
9
pH 6.0: about 65% of maximal activity, pH 9.0: about 40% of maximal activity
Escherichia coli
Other publictions for EC 2.3.1.181
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)
726128
Ewald
Two redundant octanoyltransfer ...
Arabidopsis thaliana
Plant Biol.
16
35-42
2014
-
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1
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2
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1
2
-
-
-
737026
Ewald
Lipoate-protein ligase and oct ...
Arabidopsis thaliana
Plant Physiol.
165
978-990
2014
-
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-
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1
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1
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3
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737308
Hermes
The role of the Saccharomyces ...
Saccharomyces cerevisiae
Yeast
30
415-427
2013
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5
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1
1
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712504
Hassan
Protein-protein interactions i ...
Escherichia coli
J. Biol. Chem.
286
8263-8276
2011
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1
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1
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2
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1
1
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718133
Martin
A novel two-gene requirement f ...
Bacillus subtilis
Mol. Microbiol.
80
335-349
2011
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1
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1
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2
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718134
Christensen
A novel amidotransferase requi ...
Bacillus subtilis
Mol. Microbiol.
80
350-363
2011
1
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1
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2
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711217
Christensen
Lipoic acid synthesis: a new f ...
Bacillus subtilis
Biochemistry
49
10024-10036
2010
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1
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4
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1
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5
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1
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1
1
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1
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1
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4
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1
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1
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1
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704311
Hermes
Scavenging of cytosolic octano ...
Escherichia coli
J. Bacteriol.
191
6796-6803
2009
-
-
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1
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1
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2
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1
1
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706425
Guenther
Knockout studies reveal an imp ...
Plasmodium falciparum
PLoS ONE
4
e5510
2009
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6
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1
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688368
Fujiwara
Crystal structure of bovine li ...
Bos taurus
J. Mol. Biol.
371
222-234
2007
-
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1
1
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1
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1
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4
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676872
Ma
The Mycobacterium tuberculosis ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Proc. Natl. Acad. Sci. USA
103
8662-8667
2006
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661184
Zhao
The reaction of LipB, the octa ...
Escherichia coli
Biochemistry
44
16737-16746
2005
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663308
Nesbitt
Expression, purification, and ...
Escherichia coli
Protein Expr. Purif.
39
269-282
2005
2
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1
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662002
Jordan
The Escherichia coli lipB gene ...
Escherichia coli
J. Bacteriol.
185
1582-1589
2003
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663062
Wada
Lipoic acid metabolism in Arab ...
Arabidopsis thaliana
Plant Cell Physiol.
42
650-656
2001
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662098
Jordan
A new metabolic link. The acyl ...
Escherichia coli, Neurospora crassa, Pisum sativum
J. Biol. Chem.
272
17903-17906
1997
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661982
vanden Boom
Lipoic acid metabolism in Esch ...
Escherichia coli
J. Bacteriol.
173
6411-6420
1991
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