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ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
-
-
-
-
ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
kinetic ordered bi uni uni bi ping-pong mechanism
ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
bi uni uni bi ping-pong kinetic mechanism
-
ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
bi uni uni bi ping-pong kinetic mechanism
-
ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
bi uni uni bi ping-pong kinetic mechanism
-
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
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
-
-
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4-[2-(trifluoromethyl)phenyl]-4-oxobutyric acid + CoA
AMP + diphosphate + 4-[2-(trifluoromethyl)phenyl]-4-oxobutyryl-CoA
a substrate analogue, 100fold less active than 2-succinylbenzoate
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
ATP + 2-succinylbenzoate + dephospho-CoA
AMP + 2-succinylbenzoyldephospho-CoA + diphosphate
-
96% of the activity with CoA
-
-
?
ATP + benzoylpropionic acid + CoA
AMP + benzoylpropionyl-CoA + diphosphate
-
21.6% of the activity with o-succinylbenzoate
-
-
?
ATP + o-malonylbenzoate + CoA
AMP + o-malonylbenzoyl-CoA + diphosphate
-
11.6% of the activity with o-succinylnemzoate
-
-
?
CTP + o-succinylbenzoate + CoA
CMP + diphosphate + o-succinylbenzoyl-CoA
-
13.5% of the activity with ATP
-
-
?
GTP + o-succinylbenzoate + CoA
GMP + diphosphate + o-succinylbenzoyl-CoA
-
13.4% of the activity with ATP
-
-
?
ITP + o-succinylbenzoate + CoA
IMP + diphosphate + o-succinylbenzoyl-CoA
-
10.9% of the activity with ATP
-
-
?
TTP + o-succinylbenzoate + CoA
TMP + diphosphate + o-succinylbenzoyl-CoA
-
12.1% of the activity with ATP
-
-
?
UTP + o-succinylbenzoate + CoA
UMP + diphosphate + o-succinylbenzoyl-CoA
-
12.3% of the activity with ATP
-
-
?
additional information
?
-
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
OSB-CoA ligase acts in phylloquinone synthesis, pathway for phylloquinone synthesis, overview
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-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
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
substrate specificity and binding structure, overview
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
-
o-succinylbenzoyl-CoA is a highly unstable compound which spontaneously converts to o-succinylbenzoate-spirolactone in absence of 1,4-dihydroxy-2-naphthoic acid synthase
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
o-succinylbenzoyl-CoA is an intermediate in menaquinone (vitamin K2) biosynthesis
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
o-succinylbenzoyl-CoA is an intermediate in menaquinone (vitamin K2) biosynthesis
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
-
the o-succinylbenzoyl conenzyme A ester is unstable at alkaline and neutral pH, but is fairly stable under acid conditions
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
-
incubation of the purified enzyme at different pH values gives a varying ratio of o-succinylbenzoyl-CoA to o-succinylbenzoyl-diCoA. No formation of o-succinylbenzoyl-2-CoA. No formation of ADP
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
-
the o-succinylbenzoyl-CoA derivative is rather unstable, under a variety of conditions it is converted to a spirodilactone form of o-succinylbenzoate
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
o-succinylbenzoyl-CoA is an intermediate in menaquinone (vitamin K2) biosynthesis
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
o-succinylbenzoyl-CoA is an intermediate in menaquinone (vitamin K2) biosynthesis
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
o-succinylbenzoyl-CoA is an intermediate in menaquinone (vitamin K2) biosynthesis
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
-
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
-
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
-
-
-
-
?
additional information
?
-
-
His341 plays an important role in catalysis since it is probably involved in the binding of ATP to the enzyme
-
-
?
additional information
?
-
-
no activity with: o-malonylbenzoic acid, benzoylpropionic acid, benzoic acid, o-acetylbenzoic acid, phthalic acid and p-coumaric acid
-
-
?
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ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
OSB-CoA ligase acts in phylloquinone synthesis, pathway for phylloquinone synthesis, overview
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-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
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
o-succinylbenzoyl-CoA is an intermediate in menaquinone (vitamin K2) biosynthesis
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
o-succinylbenzoyl-CoA is an intermediate in menaquinone (vitamin K2) biosynthesis
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
o-succinylbenzoyl-CoA is an intermediate in menaquinone (vitamin K2) biosynthesis
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
o-succinylbenzoyl-CoA is an intermediate in menaquinone (vitamin K2) biosynthesis
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
o-succinylbenzoyl-CoA is an intermediate in menaquinone (vitamin K2) biosynthesis
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
-
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
-
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
-
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
5'-([[(1E)-5-(2-carboxyphenyl)-5-oxopent-1-en-1-yl]sulfonyl]amino)-5'-deoxyadenosine
-
-
5'-([[(1E)-5-(2-carboxyphenyl)-5-oxopent-1-en-1-yl]sulfonyl]amino)-5'-deoxyadenosine
-
-
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'-([[(1E)-5-(2-carboxyphenyl)pent-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)-4-oxobutanoyl]sulfamoyl]amino)-5'-deoxyadenosine
-
-
5'-([[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]amino)-5'-deoxyadenosine
-
-
5'-([[4-(2-carboxyphenyl)butanoyl]sulfamoyl]amino)-5'-deoxyadenosine
-
-
5'-([[4-(2-carboxyphenyl)butanoyl]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]-5-oxopent-1-en-1-yl]sulfonyl)amino]adenosine
-
-
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'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]pent-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]-4-oxobutanoyl]sulfamoyl)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'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]butanoyl]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]-4-oxobutanoyl]sulfamoyl)adenosine
-
-
5'-O-([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)adenosine
-
-
5'-O-([4-[2-(methoxycarbonyl)phenyl]butanoyl]sulfamoyl)adenosine
-
hydrolytically unstable at the acyl sulfamate moiety
5'-O-([4-[2-(methoxycarbonyl)phenyl]butanoyl]sulfamoyl)adenosine
-
-
5'-O-([4-[2-(methoxycarbonyl)phenyl]butanoyl]sulfamoyl)adenosine
-
hydrolytically unstable at the acyl sulfamate moiety
5'-O-[[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]adenosine
-
-
5'-O-[[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]adenosine
-
sulfonyladenosine analogue of the cognate reaction intermediate, o-succinylbenzoate-AMP, competitive inhibitor of mtMenE with respect to ATP and a noncompetitive inhibitor with respect to 2-succinylbenzoate
5'-O-[[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]adenosine
-
sulfonyladenosine analogue of the cognate reaction intermediate, o-succinylbenzoate-AMP. Putative active site residues, Arg222 and Ser302, may interact with the 2-succinylbenzoate aromatic carboxylate and bind the 2-succinylbenzoate ketone oxygen, respectively, computational docking of 2-succinylbenzoate-AMP with the unliganded crystal structure of saMenE
5'-O-[[4-(2-carboxyphenyl)butanoyl]sulfamoyl]adenosine
-
-
5'-O-[[4-(2-carboxyphenyl)butanoyl]sulfamoyl]adenosine
-
-
5'-O-[[4-(2-carboxyphenyl)butanoyl]sulfamoyl]adenosine
-
-
additional information
inhibitor design studies, overvew
-
additional information
-
inhibitor design studies, overvew
-
additional information
-
structure-function relationship of o-succinylbenzoate-AMP sulfonyladenosine analogue inhibitors, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.0219 - 0.88
2-succinylbenzoate
0.016 - 0.1481
o-succinylbenzoate
additional information
additional information
-
0.0219
2-succinylbenzoate
pH 7.5, 21°C, recombinant His-tagged enzyme
0.044
2-succinylbenzoate
pH 7.5, 24°C, recombinant wild-type enzyme
0.057
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant R382A
0.066
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant R382K
0.08
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant G157P
0.087
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant T155A
0.12
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant G154P
0.14
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant T156A
0.28
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant T155A/T156A
0.88
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant T152A
0.024
ATP
pH 7.5, 24°C, recombinant wild-type enzyme
0.0268
ATP
pH 7.5, 21°C, recombinant His-tagged enzyme
0.0735
ATP
-
native enzyme
0.4
ATP
-
mutant enzyme H341A
2.3
ATP
pH 7.5, 24°C, recombinant mutant T156A
3.17
ATP
pH 7.5, 24°C, recombinant mutant G157P
3.3
ATP
pH 7.5, 24°C, recombinant mutant T155A/T156A
3.4
ATP
pH 7.5, 24°C, recombinant mutant G154P
3.5
ATP
pH 7.5, 24°C, recombinant mutant T152A
4.2
ATP
pH 7.5, 24°C, recombinant mutant T155A
4.67
ATP
pH 7.5, 24°C, recombinant mutant R382K
8.5
ATP
pH 7.5, 24°C, recombinant mutant R382A
0.0165
CoA
-
pH 7.2, 30°C
0.17
CoA
pH 7.5, 24°C, recombinant mutant T155A/T156A
0.21
CoA
pH 7.5, 24°C, recombinant mutant T156A
0.24
CoA
pH 7.5, 24°C, recombinant wild-type enzyme
0.25
CoA
pH 7.5, 24°C, recombinant mutant G157P
0.26
CoA
pH 7.5, 24°C, recombinant mutant T152A
0.27
CoA
pH 7.5, 24°C, recombinant mutant G154P
0.304
CoA
pH 7.5, 21°C, recombinant His-tagged enzyme
0.41
CoA
pH 7.5, 24°C, recombinant mutant T155A
2.7
CoA
pH 7.5, 24°C, recombinant mutant R382A
3
CoA
pH 7.5, 24°C, recombinant mutant R382K
0.016
o-succinylbenzoate
-
-
0.1481
o-succinylbenzoate
-
pH 7.2, 30°C
additional information
additional information
pre-steady-state and steady-state kinetic studies, overview
-
additional information
additional information
-
pre-steady-state and steady-state kinetic studies, overview
-
additional information
additional information
single-substrate kinetics
-
additional information
additional information
-
single-substrate kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.045 - 120
2-succinylbenzoate
0.045
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant T155A/T156A
0.125
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant T155A
0.137
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant T152A
0.15
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant R382A
0.213
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant T156A
0.228
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant R382K
2.17
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant G154P
2.62
2-succinylbenzoate
pH 7.5, 21°C, recombinant His-tagged enzyme
46.67
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant G157P
120
2-succinylbenzoate
pH 7.5, 24°C, recombinant wild-type enzyme
0.045
ATP
pH 7.5, 24°C, recombinant mutant T155A/T156A
0.077
ATP
pH 7.5, 24°C, recombinant mutant T155A
0.135
ATP
pH 7.5, 24°C, recombinant mutant T152A
0.163
ATP
pH 7.5, 24°C, recombinant mutant R382K
0.213
ATP
pH 7.5, 24°C, recombinant mutant T156A
0.218
ATP
pH 7.5, 24°C, recombinant mutant R382A
1.65
ATP
pH 7.5, 24°C, recombinant mutant G154P
2.62
ATP
pH 7.5, 21°C, recombinant His-tagged enzyme
3
ATP
pH 7.5, 24°C, recombinant mutant G157P
105
ATP
pH 7.5, 24°C, recombinant wild-type enzyme
0.05
CoA
pH 7.5, 24°C, recombinant mutant T155A/T156A
0.103
CoA
pH 7.5, 24°C, recombinant mutant T155A
0.145
CoA
pH 7.5, 24°C, recombinant mutant T156A
0.162
CoA
pH 7.5, 24°C, recombinant mutant R382K
0.206
CoA
pH 7.5, 24°C, recombinant mutant T152A
0.283
CoA
pH 7.5, 24°C, recombinant mutant R382A
2.17
CoA
pH 7.5, 24°C, recombinant mutant G154P
2.62
CoA
pH 7.5, 21°C, recombinant His-tagged enzyme
4.3
CoA
pH 7.5, 24°C, recombinant mutant G157P
121.7
CoA
pH 7.5, 24°C, recombinant wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0052 - 0.0089
5'-O-(N-[2-(trifluoromethyl)phenyl]-4-oxobutyl)adenosine sulfonamide
0.0054 - 0.128
5'-O-[[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]adenosine
3
benzoyl-CoA
pH 7.5, 21°C, versus CoA, recombinant enzyme
0.0052
5'-O-(N-[2-(trifluoromethyl)phenyl]-4-oxobutyl)adenosine sulfonamide
pH 7.5, 21°C, versus ATP, recombinant enzyme
0.0056
5'-O-(N-[2-(trifluoromethyl)phenyl]-4-oxobutyl)adenosine sulfonamide
pH 7.5, 21°C, versus 2-succinylbenzoate, recombinant enzyme
0.0089
5'-O-(N-[2-(trifluoromethyl)phenyl]-4-oxobutyl)adenosine sulfonamide
pH 7.5, 21°C, versus CoA, recombinant enzyme
0.0054
5'-O-[[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]adenosine
-
versus ATP, pH and temperature not specified in the publication
0.0112
5'-O-[[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]adenosine
-
versus 2-succinylbenzoate, pH and temperature not specified in the publication
0.022
5'-O-[[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]adenosine
-
pH and temperature not specified in the publication
0.128
5'-O-[[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]adenosine
-
pH and temperature not specified in the publication
3.6
AMP
pH 7.5, 21°C, versus ATP, recombinant enzyme
4.6
AMP
pH 7.5, 21°C, versus 2-succinylbenzoate, recombinant enzyme
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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
0.00016
5'-([[(1E)-5-(2-carboxyphenyl)-5-oxopent-1-en-1-yl]sulfonyl]amino)-5'-deoxyadenosine
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.00033
5'-([[(1E)-5-(2-carboxyphenyl)-5-oxopent-1-en-1-yl]sulfonyl]amino)-5'-deoxyadenosine
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.00057
5'-([[(1E)-5-(2-carboxyphenyl)-5-oxopent-1-en-1-yl]sulfonyl]amino)-5'-deoxyadenosine
Escherichia coli
-
pH and temperature not specified in the publication
0.0316
5'-([[(1E)-5-(2-carboxyphenyl)pent-1-en-1-yl]sulfonyl]amino)-5'-deoxyadenosine
Escherichia coli
-
pH and temperature not specified in the publication
0.0544
5'-([[(1E)-5-(2-carboxyphenyl)pent-1-en-1-yl]sulfonyl]amino)-5'-deoxyadenosine
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.106
5'-([[(1E)-5-(2-carboxyphenyl)pent-1-en-1-yl]sulfonyl]amino)-5'-deoxyadenosine
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0002
5'-([[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]amino)-5'-deoxyadenosine
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.00024
5'-([[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]amino)-5'-deoxyadenosine
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.00063
5'-([[4-(2-carboxyphenyl)-4-oxobutanoyl]sulfamoyl]amino)-5'-deoxyadenosine
Escherichia coli
-
pH and temperature not specified in the publication
0.085
5'-([[4-(2-carboxyphenyl)butanoyl]sulfamoyl]amino)-5'-deoxyadenosine
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.101
5'-([[4-(2-carboxyphenyl)butanoyl]sulfamoyl]amino)-5'-deoxyadenosine
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0057
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]-5-oxopent-1-en-1-yl]sulfonyl)amino]adenosine
Escherichia coli
-
pH and temperature not specified in the publication
0.0457
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]-5-oxopent-1-en-1-yl]sulfonyl)amino]adenosine
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.117
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]-5-oxopent-1-en-1-yl]sulfonyl)amino]adenosine
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.2
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]pent-1-en-1-yl]sulfonyl)amino]adenosine
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.2
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]pent-1-en-1-yl]sulfonyl)amino]adenosine
Escherichia coli
-
pH and temperature not specified in the publication
0.2
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]pent-1-en-1-yl]sulfonyl)amino]adenosine
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0235
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)amino]adenosine
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0341
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)amino]adenosine
Escherichia coli
-
pH and temperature not specified in the publication
0.2
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)amino]adenosine
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.2
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]butanoyl]sulfamoyl)amino]adenosine
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.2
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]butanoyl]sulfamoyl)amino]adenosine
Escherichia coli
-
pH and temperature not specified in the publication
0.2
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]butanoyl]sulfamoyl)amino]adenosine
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0142
5'-O-([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)adenosine
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0246
5'-O-([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)adenosine
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.038
5'-O-([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)adenosine
Escherichia coli
-
pH and temperature not specified in the publication
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metabolism
o-succinylbenzoyl-CoA synthetase, or MenE, is an essential adenylate-forming enzyme in the menaquinone biosynthesis
metabolism
-
o-succinylbenzoyl-CoA synthetase, or MenE, is an essential adenylate-forming enzyme in the menaquinone biosynthesis
-
physiological function
-
the enzyme is essential in Escherichia coli and is involved in menaquinone biosynthesis
physiological function
-
the enzyme is essential in Mycobacterium tuberculosis and is involved in menaquinone biosynthesis
physiological function
-
the enzyme is important in Mycobacterium tuberculosis
physiological function
ATP-dependent configuration of adenylation active site in o-succinylbenzoyl-CoA synthetase
physiological function
-
ATP-dependent configuration of adenylation active site in o-succinylbenzoyl-CoA synthetase
-
additional information
-
the basic residue, Arg222, may interact with the aromatic carboxylate of 2-succinylbenzoate
additional information
-
the basic residue, Arg222, may interact with the aromatic carboxylate of 2-succinylbenzoate
additional information
-
the basic residue, Arg222, may interact with the aromatic carboxylate of 2-succinylbenzoate
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
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
-
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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
R382A
-
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
-
T156A
-
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
-
H341A
-
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
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
additional information
-
mutation of the P-loop residues hydrogen-bonded to ATP reveals a crucial catalytic role of ATP-enzyme interaction
-
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Meganathan, R.; Bentley, R.
Menaquinone (vitamin K2) biosynthesis: conversion of o-succinylbenzoic acid to 1,4-dihydroxy-2-naphthoic acid by Mycobacterium phlei enzymes
J. Bacteriol.
140
92-98
1979
Mycolicibacterium phlei
brenda
Kolkmann, R.; Leistner, E.
4-(2'-Carboxyphenyl)-4-oxobutyryl coenzyme A ester, an intermediate in vitamin K2 (menaquinone) biosynthesis
Z. Naturforsch. C
42
1207-1214
1987
Escherichia coli, Mycolicibacterium phlei
brenda
Heide, L.; Leistner, E.
Enzymatic synthesis of the coenzyme A ester of o-succinylbenzoic acid, an intermediate in menaquinone (vitamin K2) biosynthesis
FEBS Lett.
128
201-204
1981
Mycolicibacterium phlei
brenda
Shaw, D.J.; Robinson, E.C.; Meganathan, R.; Bentley, R.; Guest, J.R.
Recombinent plasmids containing menaquinone biosynthetic genes of Escherichia coli
FEMS Microbiol. Lett.
17
63-67
1983
Escherichia coli
-
brenda
Heide, L.; Arendt, S.; Leistner, E.
Enzymatic synthesis, characterization, and metabolism of the coenzyme A ester of o-succinylbenzoic acid, an intermediate in menaquinone (vitamin K2) biosynthesis
J. Biol. Chem.
257
7396-7400
1982
Mycolicibacterium phlei
brenda
Johnson, T.W.; Naithani, S.; Stewart, C.Jr.; Zybailov, B.; Jones, A.D.; Golbeck, J.H.; Chitnis, P.R.
The menD and menE homologs code for 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylate synthase and O-succinylbenzoic acid-CoA synthase in the phylloquinone biosynthetic pathway of Synechocystis sp. PCC 6803
Biochim. Biophys. Acta
1557
67-76
2003
Synechocystis sp.
brenda
Siewecke, H.J.; Leistner, E.
O-Succinylbenzoate:coenzyme A ligase, an enzyme involved in menaquinone (vitamin K2) biosynthesis displays braod specificity
Z. Naturforsch. C
46
585-590
1991
Mycolicibacterium phlei
brenda
Bhattacharyya, D.K.; Kwon, O.; Meganathan, R.
Vitamin K2 (menaquinone) biosynthesis in Escherichia coli: evidence for the presence of an essential histidine residue in o-succinylbenzoyl coenzyme A synthetase
J. Bacteriol.
179
6061-6065
1997
Escherichia coli
brenda
Kwon, O.; Bhattacharyya, D.K.; Meganathan, R.
Menaquinone (vitamin K2) biosynthesis: overexpression, purification, and properties of o-succinylbenzoyl-coenzyme A synthetase from Escherichia coli
J. Bacteriol.
178
6778-6781
1996
Escherichia coli
brenda
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
brenda
Kim, H.U.; van Oostende, C.; Basset, G.J.; Browse, J.
The AAE14 gene encodes the Arabidopsis o-succinylbenzoyl-CoA ligase that is essential for phylloquinone synthesis and photosystem-I function
Plant J.
54
272-283
2008
Arabidopsis thaliana (Q8VYJ1)
brenda
Lu, X.; Zhou, R.; Sharma, I.; Li, X.; Kumar, G.; Swaminathan, S.; Tonge, P.J.; Tan, D.S.
Stable analogues of OSB-AMP: potent inhibitors of MenE, the o-succinylbenzoate-CoA synthetase from bacterial menaquinone biosynthesis
ChemBioChem
13
129-136
2012
Escherichia coli, Staphylococcus aureus, Mycobacterium tuberculosis
brenda
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)
brenda