BRENDA - Enzyme Database show
show all sequences of 2.8.1.8

Lipoic acid synthesis: a new family of octanoyltransferases generally annotated as lipoate protein ligases

Christensen, Q.H.; Cronan, J.E.; Biochemistry 49, 10024-10036 (2010)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
protein N6-(octanoyl)lysine + sulfur + S-adenosyl-L-methionine
Bacillus subtilis
-
protein N6-(lipoyl)lysine + L-methionine + 5'-deoxyadenosine
-
-
ir
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
protein N6-(octanoyl)lysine + sulfur + S-adenosyl-L-methionine
-
711217
Bacillus subtilis
protein N6-(lipoyl)lysine + L-methionine + 5'-deoxyadenosine
-
-
-
ir
Cofactor
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Bacillus subtilis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Bacillus subtilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
protein N6-(octanoyl)lysine + sulfur + S-adenosyl-L-methionine
Bacillus subtilis
-
protein N6-(lipoyl)lysine + L-methionine + 5'-deoxyadenosine
-
-
ir
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
protein N6-(octanoyl)lysine + sulfur + S-adenosyl-L-methionine
-
711217
Bacillus subtilis
protein N6-(lipoyl)lysine + L-methionine + 5'-deoxyadenosine
-
-
-
ir
Other publictions for EC 2.8.1.8
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)
737720
Lanz
Characterization of Lipoyl Syn ...
Mycobacterium tuberculosis
Biochemistry
55
1372-1383
2016
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739557
McLaughlin
Crystallographic snapshots of ...
Mycobacterium tuberculosis
Proc. Natl. Acad. Sci. USA
113
9446-9450
2016
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726128
Ewald
Two redundant octanoyltransfer ...
Arabidopsis thaliana
Plant Biol.
16
35-42
2014
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737696
Lanz
Evidence for a catalytically a ...
Escherichia coli, Thermus thermophilus
Biochemistry
53
4557-4572
2014
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718133
Martin
A novel two-gene requirement f ...
Bacillus subtilis
Mol. Microbiol.
80
335-349
2011
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711217
Christensen
Lipoic acid synthesis: a new f ...
Bacillus subtilis
Biochemistry
49
10024-10036
2010
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660704
Bryant
The activity of a thermostable ...
Saccharolobus solfataricus
Anal. Biochem.
351
44-49
2006
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671329
Douglas
Lipoyl synthase inserts sulfur ...
Saccharolobus solfataricus
Angew. Chem.
45
5197-5199
2006
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661945
Cicchillo
Mechanistic investigations of ...
Escherichia coli
J. Am. Chem. Soc.
127
2860-2861
2005
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661138
Cicchillo
Lipoyl synthase requires two e ...
Escherichia coli
Biochemistry
43
6378-6386
2004
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661463
Zhao
Assembly of the covalent linka ...
Escherichia coli
Chem. Biol.
10
1293-1302
2003
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661727
Thomsen-Zieger
Apicomplexan parasites contain ...
Toxoplasma gondii
FEBS Lett.
547
80-86
2003
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663290
Kriek
Effect of iron-sulfur cluster ...
Escherichia coli
Protein Expr. Purif.
28
241-245
2003
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661057
Miller
Escherichia coli LipA is a lip ...
Escherichia coli
Biochemistry
39
15166-15178
2000
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661718
Ollagnier-de Choudens
The lipoate synthase from Esch ...
Escherichia coli
FEBS Lett.
453
25-28
1999
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662098
Jordan
A new metabolic link. The acyl ...
Escherichia coli, Neurospora crassa, Pisum sativum
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272
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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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