Information on EC 6.2.1.26 - O-succinylbenzoate-CoA ligase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
6.2.1.26
-
RECOMMENDED NAME
GeneOntology No.
O-succinylbenzoate-CoA ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
forming of carbon sulfur bonds
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,4-dihydroxy-2-naphthoate biosynthesis
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Biosynthesis of secondary metabolites
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Metabolic pathways
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Ubiquinone and other terpenoid-quinone biosynthesis
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vitamin K metabolism
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SYSTEMATIC NAME
IUBMB Comments
2-succinylbenzoate:CoA ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
72506-70-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene AAE14
UniProt
Manually annotated by BRENDA team
gene menE
UniProt
Manually annotated by BRENDA team
PCC 6803
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-[2-(trifluoromethyl)phenyl]-4-oxobutyric acid + CoA
AMP + diphosphate + 4-[2-(trifluoromethyl)phenyl]-4-oxobutyryl-CoA
show the reaction diagram
a substrate analogue, 100fold less active than 2-succinylbenzoate
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
show the reaction diagram
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
show the reaction diagram
ATP + 2-succinylbenzoate + dephospho-CoA
AMP + 2-succinylbenzoyldephospho-CoA + diphosphate
show the reaction diagram
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96% of the activity with CoA
-
-
?
ATP + benzoylpropionic acid + CoA
AMP + benzoylpropionyl-CoA + diphosphate
show the reaction diagram
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21.6% of the activity with o-succinylbenzoate
-
-
?
ATP + o-malonylbenzoate + CoA
AMP + o-malonylbenzoyl-CoA + diphosphate
show the reaction diagram
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11.6% of the activity with o-succinylnemzoate
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-
?
CTP + o-succinylbenzoate + CoA
CMP + diphosphate + o-succinylbenzoyl-CoA
show the reaction diagram
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13.5% of the activity with ATP
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-
?
GTP + o-succinylbenzoate + CoA
GMP + diphosphate + o-succinylbenzoyl-CoA
show the reaction diagram
-
13.4% of the activity with ATP
-
-
?
ITP + o-succinylbenzoate + CoA
IMP + diphosphate + o-succinylbenzoyl-CoA
show the reaction diagram
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10.9% of the activity with ATP
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-
?
TTP + o-succinylbenzoate + CoA
TMP + diphosphate + o-succinylbenzoyl-CoA
show the reaction diagram
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12.1% of the activity with ATP
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-
?
UTP + o-succinylbenzoate + CoA
UMP + diphosphate + o-succinylbenzoyl-CoA
show the reaction diagram
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12.3% of the activity with ATP
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?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
show the reaction diagram
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
7% of the activation with Mg2+
K+
-
0.5 mM, 1 mM or 5 mM, approximately twofold higher activity than the control
Na+
-
0.5 mM, 1 mM or 5 mM, approximately twofold higher activity than the control
Ni2+
-
46% of the activation with Mg2+
Zn2+
-
0.5 mM, 1 mM or 5 mM, approximately twofold higher activity than the control
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-([[(1E)-5-(2-carboxyphenyl)-5-oxopent-1-en-1-yl]sulfonyl]amino)-5'-deoxyadenosine
5'-([[(1E)-5-(2-carboxyphenyl)pent-1-en-1-yl]sulfonyl]amino)-5'-deoxyadenosine
5'-([[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]amino)-5'-deoxyadenosine
5'-([[4-(2-carboxyphenyl)butanoyl]sulfamoyl]amino)-5'-deoxyadenosine
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]-5-oxopent-1-en-1-yl]sulfonyl)amino]adenosine
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]pent-1-en-1-yl]sulfonyl)amino]adenosine
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)amino]adenosine
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]butanoyl]sulfamoyl)amino]adenosine
5'-O-([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)adenosine
5'-O-([4-[2-(methoxycarbonyl)phenyl]butanoyl]sulfamoyl)adenosine
5'-O-[[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]adenosine
5'-O-[[4-(2-carboxyphenyl)butanoyl]sulfamoyl]adenosine
5'-O-{N-[2-(trifluoromethyl)phenyl]-4-oxobutyl}adenosine sulfonamide
i.e. TFMP-butyl-AMS, a reaction intermediate analogue of 2-succinylbenzoate-AMP, uncompetitive versus CoA and a mixed-type versus ATP and 2-succinylbenzoate
AMP
competitive versus ATP, mixed-type versus 2-succinylbenzoate
benzoyl-CoA
competitive versus CoA
Diethylpyrocarbonate
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inactivation follows pseudo-first-order kinetics with a second-order rate constant of 0.00092 /min *microM, partial protection from inactivation by either o-succinylbenzoic acid, ATP, or ATP plus Mg2+ while inactivation is completely prevented by the presence of the combination of ATP, Mg2+ and o-succinylbenzoate
Mg2+
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above 1 mM
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
CoA, the last substrate to bind, strongly activates the first half-reaction after the first round of turnover, by CoA stabilizing conformations of the enzyme in the F form, which slowly isomerize back to the E form
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0219
2-sucinylbenzoate
pH 7.5, 21C, recombinant His-tagged enzyme
-
0.0268 - 0.4
ATP
0.0165 - 0.36
CoA
0.016 - 0.1481
o-succinylbenzoate
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.62
2-sucinylbenzoate
Bacillus anthracis
Q81K97
pH 7.5, 21C, recombinant His-tagged enzyme
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2.62
ATP
Bacillus anthracis
Q81K97
pH 7.5, 21C, recombinant His-tagged enzyme
2.62
CoA
Bacillus anthracis
Q81K97
pH 7.5, 21C, recombinant His-tagged enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0052 - 0.0089
5'-O-(N-[2-(trifluoromethyl)phenyl]-4-oxobutyl)adenosine sulfonamide
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0.0054 - 0.128
5'-O-[[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]adenosine
3.6 - 4.6
AMP
3
benzoyl-CoA
pH 7.5, 21C, versus CoA, recombinant enzyme
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00016 - 0.00057
5'-([[(1E)-5-(2-carboxyphenyl)-5-oxopent-1-en-1-yl]sulfonyl]amino)-5'-deoxyadenosine
0.0316 - 0.106
5'-([[(1E)-5-(2-carboxyphenyl)pent-1-en-1-yl]sulfonyl]amino)-5'-deoxyadenosine
0.0002 - 0.00063
5'-([[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]amino)-5'-deoxyadenosine
0.085 - 0.101
5'-([[4-(2-carboxyphenyl)butanoyl]sulfamoyl]amino)-5'-deoxyadenosine
0.0057 - 0.117
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]-5-oxopent-1-en-1-yl]sulfonyl)amino]adenosine
0.2
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]pent-1-en-1-yl]sulfonyl)amino]adenosine
0.0235 - 0.2
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)amino]adenosine
0.2
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]butanoyl]sulfamoyl)amino]adenosine
0.0142 - 0.038
5'-O-([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)adenosine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
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pH 6.5: 55% of maximal activity, pH 8.5: 80% of maximnal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Escherichia coli (strain K12)
Staphylococcus aureus (strain Newman)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
gel filtration
49000
-
4 * 49000, SDS-PAGE
185000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 49000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and hydrophobic interaction chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene AAE14, complementates an Escherichia coli mutant disrupted in the menE gene encoding the enzyme, and restores menaquinone biosynthesis
gene menE, DNA and amino acid sequence determination and analysis, expression of the His6-tagged enzyme in Escherichia coli strain BL21(DE3)
isolation of two CoE1-men+ hybrid plasmids, one of which contains the entire menD gene. Alignment of the genetic and restriction site maps of the men region and the amplification of menaquinone biosynthetic enzyme activities in plasmid-carrying strains
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H341A
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mutant enzyme loses 65% of ist activity and the Km-value for ATP increases 5.4fold
additional information
identification of three aae14 mutant alleles by reverse genetics, that are seedling lethal, and show no detectable phylloquinon, phenotype, overview. Weak expression of an AAE14 transgene in mutant Arabidopsis thaliana plants, controlled by the uninduced XVE promoter, results in chlorotic, slow-growing plants that accumulate phylloquinone. Inducing the XVE promoter in these plants, or expressing an AAE14 transgene under the control of the CaMV 35S promoter, led to full complementation of the mutant phenotype, aae14-mutant plants are also able to synthesize phylloquinone when provided with 1,4-dihydroxy-2-naphthoate, an intermediate in phylloquinone synthesis downstream of the OSB-CoA ligase reaction, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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