Any feedback?
Information on EC 6.2.1.26 - O-succinylbenzoate-CoA ligase and Organism(s) Bacillus subtilis and UniProt Accession P23971
for references in articles please use BRENDA:EC6.2.1.26Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
6.2.1.26 O-succinylbenzoate-CoA ligaseSpecify your search results
Word Map
- 6.2.1.26
- menaquinone
-
o-succinylbenzoic
-
1,4-dihydroxy-2-naphthoic
-
half-reaction
- drug development
- anthracis
-
semi-automated
-
wells
- 5'-triphosphate
-
mono-phosphate
- adenylyltransferase
- phylloquinone
-
backside
-
benzoic
- mononucleotide
- phlei
-
dihydroxynaphthoate
-
in-line
-
unattended
-
ping-pong
- isochorismate
-
ultra-high
-
thioesterification
-
scalable
-
liquid-handling
- malachite
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
O-succinylbenzoate-CoA synthase
-
-
-
-
o-succinylbenzoyl-coenzyme A synthetase
-
-
-
-
OSB-CoA synthetase
-
-
-
-
OSB:CoA ligase
-
-
-
-
synthetase, o-succinylbenzoyl coenzyme A
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
the enzyme adopts an ordered bi uni uni bi ping-pong mechanism, which involves ATP as the first binding substrate and a large conformational change during the catalysis. In MenE catalysis, tight gripping interactions of the phosphate-binding loop (P-loop) with the ATP triphosphate moiety and an open-closed conformational change to form a compact adenylation active site create a new binding site for the carboxylate substrate. Analysis of the adenylation half-reaction in the domain alteration catalytic mechanism of the adenylateforming enzymes, open-closed conformational change in ATP configuration of the adenylation active site
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
forming of carbon sulfur bonds
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
2-succinylbenzoate:CoA ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
72506-70-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.28
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant T155A/T156A
additional information
additional information
single-substrate kinetics
-
additional information
additional information
-
single-substrate kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.045
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant T155A/T156A
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
o-succinylbenzoyl-CoA synthetase, or MenE, is an essential adenylate-forming enzyme in the menaquinone biosynthesis
physiological function
ATP-dependent configuration of adenylation active site in o-succinylbenzoyl-CoA synthetase
additional information
additional information
in MenE catalysis, tight gripping interactions of the phosphate-binding loop (P-loop) with the ATP triphosphate moiety and an open-closed conformational change to form a compact adenylation active site create a new binding site for the carboxylate substrate, allowing revelation of the determinants of substrate specificities and in-line alignment of the two substrates for backside nucleophilic substitution reaction by molecular modeling, overview. The ATP-enzyme interaction is suggested to play a crucial catalytic role. positioning and catalytic role of a conserved lysine residue in stabilization of the transition state, molecular docking, overview
additional information
-
in MenE catalysis, tight gripping interactions of the phosphate-binding loop (P-loop) with the ATP triphosphate moiety and an open-closed conformational change to form a compact adenylation active site create a new binding site for the carboxylate substrate, allowing revelation of the determinants of substrate specificities and in-line alignment of the two substrates for backside nucleophilic substitution reaction by molecular modeling, overview. The ATP-enzyme interaction is suggested to play a crucial catalytic role. positioning and catalytic role of a conserved lysine residue in stabilization of the transition state, molecular docking, overview
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme BsMenE, hanging drop vapor diffusion method, 1:1 mixture of a solution of protein at 10 mg/ml and a reservoir solution at pH 6.15 containing 8.1% w/v PEG 8000, 0.09 M cacodylate/HCl, 0.144 M calcium acetate, 12.6% glycerol, 0.049 M sodium phosphate monobasic, and 0.091 M dibasic potassium phosphate, a BsMenE-ATP-Mg2-complex is grown within a week in a 1:1 mixture of a solution of 10 mg/ml BsMenE protein preincubated with 3 mM ATP and 5 mM MgCl2 and a reservoir solution at pH 7.7 containing 7.2% v/v ethylene glycol, 9.9% w/v PEG 8000, 0.09 M HEPES, 3.5% v/v 2-methyl-2,4-pentanediol, and 0.01 M acetate, and a BsMenE-AMP complex grown from an 1:1 mixture of a solution of 10 mg/ml BsMenE protein preincubated with 3 mM AMP and mixed with a reservoir solution at pH 7.5 containing 0.10 M HEPES, 10% w/v PEG 6000, 5% v/v 2-methyl-2,4-pentadiol, 16°C, X-ray diffraction structure determination and analysis at 1.98-2.82 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G154P
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
G157P
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
R382A
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
R382K
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
T152A
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
T155A
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
T155A/T156A
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
T156A
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
additional information
additional information
mutation of the P-loop residues hydrogen-bonded to ATP reveals a crucial catalytic role of ATP-enzyme interaction
additional information
-
mutation of the P-loop residues hydrogen-bonded to ATP reveals a crucial catalytic role of ATP-enzyme interaction
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
o-succinylbenzoyl-CoA synthetase, or MenE, is an essential adenylate-forming enzyme targeted for development of antibiotics in the menaquinone biosynthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, Y.; Sun, Y.; Song, H.; Guo, Z.
Structural basis for the ATP-dependent configuration of adenylation active site in Bacillus subtilis o-succinylbenzoyl-CoA synthetase
J. Biol. Chem.
290
23971-23983
2015
Bacillus subtilis (P23971), Bacillus subtilis, Bacillus subtilis 168 (P23971)
EXTERNAL LINKS (specific for EC-Number 6.2.1.26)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
