BRENDA - Enzyme Database
show all sequences of 2.3.1.204

Unravelling the lipoyl-relay of exogenous lipoate utilization in Bacillus subtilis

Rasetto, N.B.; Lavatelli, A.; Martin, N.; Mansilla, M.C.; Mol. Microbiol. 112, 302-316 (2019)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
Bacillus subtilis
the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
-
?
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
Bacillus subtilis JH642
the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis JH642
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
-
757689
Bacillus subtilis
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
-
-
?
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging
757689
Bacillus subtilis
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
-
-
?
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
-
757689
Bacillus subtilis JH642
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
-
-
?
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging
757689
Bacillus subtilis JH642
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
LIPL
-
Bacillus subtilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
Bacillus subtilis
the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
-
?
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
Bacillus subtilis JH642
the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
-
757689
Bacillus subtilis
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
-
-
?
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging
757689
Bacillus subtilis
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
-
-
?
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
-
757689
Bacillus subtilis JH642
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
-
-
?
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging
757689
Bacillus subtilis JH642
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
-
-
?
General Information
General Information
Commentary
Organism
metabolism
the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging
Bacillus subtilis
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging
Bacillus subtilis
Other publictions for EC 2.3.1.204
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
Synonyms
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)
757105
Teoh
Dynamic relay of protein-boun ...
Staphylococcus aureus, Staphylococcus aureus USA300
J. Bacteriol.
201
e00446-19
2019
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1
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1
1
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757689
Rasetto
Unravelling the lipoyl-relay ...
Bacillus subtilis, Bacillus subtilis JH642
Mol. Microbiol.
112
302-316
2019
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6
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4
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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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718134
Christensen
A novel amidotransferase requi ...
Bacillus subtilis, Bacillus subtilis 168
Mol. Microbiol.
80
350-363
2011
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