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Information on EC 6.2.1.26 - O-succinylbenzoate-CoA ligase and Organism(s) Bacillus anthracis and UniProt Accession Q81K97

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.26 O-succinylbenzoate-CoA ligase
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This record set is specific for:
Bacillus anthracis
UNIPROT: Q81K97 not found.
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Word Map
The taxonomic range for the selected organisms is: Bacillus anthracis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
osb-coa synthetase, o-succinylbenzoyl-coa synthetase, aae14, osb-coa ligase, acyl-activating enzyme 14, o-succinylbenzoate-coa ligase, o-succinylbenzoate-coa synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
o-succinylbenzoyl-CoA synthetase
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OSB-CoA synthetase
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O-succinylbenzoate-CoA synthase
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-
-
-
o-succinylbenzoyl-coenzyme A synthetase
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-
-
-
OSB-CoA synthetase
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-
-
-
OSB:CoA ligase
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-
-
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synthetase, o-succinylbenzoyl coenzyme A
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
show the reaction diagram
kinetic ordered bi uni uni bi ping-pong mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
forming of carbon sulfur bonds
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-
-
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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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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
NATURAL SUBSTRATE
NATURAL PRODUCT
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-dependent condensation of o-succinylbenzoate, and CoA to form o-succinylbenzoyl-CoA, the fourth step of the menaquinone biosynthetic pathway in Bacillus anthracis
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
additional information
-
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-succinylbenzoate
pH 7.5, 21°C, recombinant His-tagged enzyme
0.0268
ATP
pH 7.5, 21°C, recombinant His-tagged enzyme
0.304
CoA
pH 7.5, 21°C, recombinant His-tagged enzyme
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.62
2-succinylbenzoate
pH 7.5, 21°C, recombinant His-tagged enzyme
2.62
ATP
pH 7.5, 21°C, recombinant His-tagged enzyme
2.62
CoA
pH 7.5, 21°C, 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
3.6 - 4.6
AMP
3
benzoyl-CoA
pH 7.5, 21°C, versus CoA, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene menE
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MENE_BACAN
481
0
53617
Swiss-Prot
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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 menE, DNA and amino acid sequence determination and analysis, expression of the His6-tagged enzyme in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the enzyme is a potential target for the discovery of antibiotics
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tian, Y.; Suk, D.H.; Cai, F.; Crich, D.; Mesecar, A.D.
Bacillus anthracis o-succinylbenzoyl-CoA synthetase: reaction kinetics and a novel inhibitor mimicking its reaction intermediate
Biochemistry
47
12434-12447
2008
Bacillus anthracis (Q81K97), Bacillus anthracis
Manually annotated by BRENDA team