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Literature summary for 6.2.1.26 extracted from

  • 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 (2008), Biochemistry, 47, 12434-12447.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.2.1.26

Activating Compound

Activating Compound Comment Organism Structure
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 Bacillus anthracis

Application

Application Comment Organism
drug development the enzyme is a potential target for the discovery of antibiotics Bacillus anthracis

Cloned(Commentary)

Cloned (Comment) Organism
gene menE, DNA and amino acid sequence determination and analysis, expression of the His6-tagged enzyme in Escherichia coli strain BL21(DE3) Bacillus anthracis

Inhibitors

Inhibitors Comment Organism Structure
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 Bacillus anthracis
AMP competitive versus ATP, mixed-type versus 2-succinylbenzoate Bacillus anthracis
benzoyl-CoA competitive versus CoA Bacillus anthracis
additional information inhibitor design studies, overvew Bacillus anthracis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information pre-steady-state and steady-state kinetic studies, overview Bacillus anthracis
0.0219
-
 2-succinylbenzoate pH 7.5, 21°C, recombinant His-tagged enzyme Bacillus anthracis
0.0268
-
 ATP pH 7.5, 21°C, recombinant His-tagged enzyme Bacillus anthracis
0.304
-
 CoA pH 7.5, 21°C, recombinant His-tagged enzyme Bacillus anthracis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Bacillus anthracis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 2-succinylbenzoate + CoA Bacillus anthracis ATP-dependent condensation of o-succinylbenzoate, and CoA to form o-succinylbenzoyl-CoA, the fourth step of the menaquinone biosynthetic pathway in Bacillus anthracis AMP + diphosphate + 2-succinylbenzoyl-CoA
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus anthracis Q81K97 gene menE
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and hydrophobic interaction chromatography Bacillus anthracis

Reaction

Reaction Comment Organism Reaction ID
ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA kinetic ordered bi uni uni bi ping-pong mechanism Bacillus anthracis
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Bacillus anthracis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-[2-(trifluoromethyl)phenyl]-4-oxobutyric acid + CoA a substrate analogue, 100fold less active than 2-succinylbenzoate Bacillus anthracis AMP + diphosphate + 4-[2-(trifluoromethyl)phenyl]-4-oxobutyryl-CoA
-
 ?
ATP + 2-succinylbenzoate + CoA ATP-dependent condensation of o-succinylbenzoate, and CoA to form o-succinylbenzoyl-CoA, the fourth step of the menaquinone biosynthetic pathway in Bacillus anthracis Bacillus anthracis AMP + diphosphate + 2-succinylbenzoyl-CoA
-
 ?
ATP + 2-succinylbenzoate + CoA substrate specificity and binding structure, overview Bacillus anthracis AMP + diphosphate + 2-succinylbenzoyl-CoA
-
 ?

Synonyms

Synonyms Comment Organism
o-succinylbenzoyl-CoA synthetase
-
 Bacillus anthracis
OSB-CoA synthetase
-
 Bacillus anthracis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
21
-
 assay at Bacillus anthracis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.62
-
 ATP pH 7.5, 21°C, recombinant His-tagged enzyme Bacillus anthracis
2.62
-
 CoA pH 7.5, 21°C, recombinant His-tagged enzyme Bacillus anthracis
2.62
-
 2-succinylbenzoate pH 7.5, 21°C, recombinant His-tagged enzyme Bacillus anthracis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Bacillus anthracis

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Bacillus anthracis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0052
-
 5'-O-(N-[2-(trifluoromethyl)phenyl]-4-oxobutyl)adenosine sulfonamide pH 7.5, 21°C, versus ATP, recombinant enzyme Bacillus anthracis
0.0056
-
 5'-O-(N-[2-(trifluoromethyl)phenyl]-4-oxobutyl)adenosine sulfonamide pH 7.5, 21°C, versus 2-succinylbenzoate, recombinant enzyme Bacillus anthracis
0.0089
-
 5'-O-(N-[2-(trifluoromethyl)phenyl]-4-oxobutyl)adenosine sulfonamide pH 7.5, 21°C, versus CoA, recombinant enzyme Bacillus anthracis
3
-
 benzoyl-CoA pH 7.5, 21°C, versus CoA, recombinant enzyme Bacillus anthracis
3.6
-
 AMP pH 7.5, 21°C, versus ATP, recombinant enzyme Bacillus anthracis
4.6
-
 AMP pH 7.5, 21°C, versus 2-succinylbenzoate, recombinant enzyme Bacillus anthracis