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show all sequences of 2.3.1.181

The role of the Saccharomyces cerevisiae lipoate protein ligase homologue, Lip3, in lipoic acid synthesis

Hermes, F.A.; Cronan, J.E.; Yeast 30, 415-427 (2013)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
Lip3 is unable to modify either lipoyl domains or glycine cleavage system 3 when provided with free octanoate, ATP and MgCl2
737308
Saccharomyces cerevisiae
?
-
-
-
-
octanoyl-CoA + [glycine cleavage system 3]-L-lysine
-
737308
Saccharomyces cerevisiae
[glycine cleavage system 3]-N6-octanoyl-L-lysine + CoA
-
-
-
?
octanoyl-CoA + [oxoglutarate dehydrogenase]-L-lysine
-
737308
Saccharomyces cerevisiae
[oxoglutarate dehydrogenase]-N6-octanoyl-L-lysine + CoA
-
-
-
?
octanoyl-CoA + [pyruvate dehydrogenase]-L-lysine
-
737308
Saccharomyces cerevisiae
[pyruvate dehydrogenase]-N6-octanoyl-L-lysine + CoA
-
-
-
?
octanoyl-[acyl-carrier protein] + [glycine cleavage system 3]-L-lysine
-
737308
Saccharomyces cerevisiae
[glycine cleavage system 3]-N6-octanoyl-L-lysine + acyl-carrier protein
in vitro reaction
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
Lip3 is unable to modify either lipoyl domains or glycine cleavage system 3 when provided with free octanoate, ATP and MgCl2
737308
Saccharomyces cerevisiae
?
-
-
-
-
octanoyl-CoA + [glycine cleavage system 3]-L-lysine
-
737308
Saccharomyces cerevisiae
[glycine cleavage system 3]-N6-octanoyl-L-lysine + CoA
-
-
-
?
octanoyl-CoA + [oxoglutarate dehydrogenase]-L-lysine
-
737308
Saccharomyces cerevisiae
[oxoglutarate dehydrogenase]-N6-octanoyl-L-lysine + CoA
-
-
-
?
octanoyl-CoA + [pyruvate dehydrogenase]-L-lysine
-
737308
Saccharomyces cerevisiae
[pyruvate dehydrogenase]-N6-octanoyl-L-lysine + CoA
-
-
-
?
octanoyl-[acyl-carrier protein] + [glycine cleavage system 3]-L-lysine
-
737308
Saccharomyces cerevisiae
[glycine cleavage system 3]-N6-octanoyl-L-lysine + acyl-carrier protein
in vitro reaction
-
-
?
General Information
General Information
Commentary
Organism
physiological function
octanoyltransferase Lip2 specifically modifies glycine cleavage system 3 using octanoyl-ACP from mitochondrial FA biosynthesis. When all glycine cleavage system 3 is octanoylated, octanoyl-ACP accumulates. An octanoyl-ACP: CoA transferase transfers the octanoyl moiety to CoA, providing substrate for octanoyltransferase Lip3 to modify pyruvate dehydrogenase and oxoglutarate dehydrogenase. Complementation of the Escherichia coli DELTAlipB DELTAlplA strain by expression of Lip3 requires a host-encoded acyl-CoA synthase
Saccharomyces cerevisiae
General Information (protein specific)
General Information
Commentary
Organism
physiological function
octanoyltransferase Lip2 specifically modifies glycine cleavage system 3 using octanoyl-ACP from mitochondrial FA biosynthesis. When all glycine cleavage system 3 is octanoylated, octanoyl-ACP accumulates. An octanoyl-ACP: CoA transferase transfers the octanoyl moiety to CoA, providing substrate for octanoyltransferase Lip3 to modify pyruvate dehydrogenase and oxoglutarate dehydrogenase. Complementation of the Escherichia coli DELTAlipB DELTAlplA strain by expression of Lip3 requires a host-encoded acyl-CoA synthase
Saccharomyces cerevisiae
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 ...
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Plant Biol.
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2014
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Hermes
The role of the Saccharomyces ...
Saccharomyces cerevisiae
Yeast
30
415-427
2013
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