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Information on EC 6.2.1.26 - O-succinylbenzoate-CoA ligase
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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 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 synthetase, o-succinylbenzoate-coa ligase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BsMenE
MenE
O-succinylbenzoate-CoA synthase
-
-
-
-
o-succinylbenzoate-CoA synthetase
o-succinylbenzoyl-CoA synthetase
o-succinylbenzoyl-coenzyme A synthetase
-
-
-
-
OSB-CoA synthetase
OSB:CoA ligase
-
-
-
-
synthetase, o-succinylbenzoyl coenzyme A
-
-
-
-
OSB-CoA synthetase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
forming of carbon sulfur bonds
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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
72506-70-8
-
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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
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 + 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
-
-
?
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
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-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
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-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
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-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
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-
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
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-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 2-succinylbenzoyl-CoA
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-
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
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-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
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-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
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-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
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-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
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-
-
-
?
ATP + 2-succinylbenzoate + CoA
AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
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-
-
-
?
additional information
?
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-
His341 plays an important role in catalysis since it is probably involved in the binding of ATP to the enzyme
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-
?
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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-
?
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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 + 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
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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
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
K+
-
0.5 mM, 1 mM or 5 mM, approximately twofold higher activity than the control
Mg2+
Mn2+
Na+
-
0.5 mM, 1 mM or 5 mM, approximately twofold higher activity than the control
Zn2+
-
0.5 mM, 1 mM or 5 mM, approximately twofold higher activity than the control
Ca2+
-
0.5 mM, 1 mM or 5 mM, approximately twofold higher activity than the control
Co2+
-
at 0.5 mM or 1.0 mM, 4fold increase in activity, 2fold increase in activity at 5 mM
Mn2+
-
at 0.5 mM or 1.0 mM, 4fold increase in activity, 2fold increase in activity at 5 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]-5-oxopent-1-en-1-yl]sulfonyl)amino]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
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'-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]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
-
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
additional information
-
structure-function relationship of o-succinylbenzoate-AMP sulfonyladenosine analogue inhibitors, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Stereoselective Synthesis, Docking, and Biological Evaluation of Difluoroindanediol-Based MenE Inhibitors as Antibiotics.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0219
2-succinylbenzoate
pH 7.5, 21°C, recombinant His-tagged enzyme
0.28
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant T155A/T156A
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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.045
2-succinylbenzoate
pH 7.5, 24°C, recombinant mutant T155A/T156A
2.62
2-succinylbenzoate
pH 7.5, 21°C, recombinant His-tagged enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0052
5'-O-(N-[2-(trifluoromethyl)phenyl]-4-oxobutyl)adenosine sulfonamide
pH 7.5, 21°C, versus ATP, recombinant enzyme